Edexcel AS Biology - Unit 1 (WBI11)

Molecules, diet, transport and health

Simplified Lecture Notes

By:
Dr. Mohab Megahed
 Table of Contents

Topic 1: Molecules, transport and health

• Transport around the body 3
• Cardiovascular diseases 12
• Biological molecules 20

Topic 2: Membranes, proteins, DNA and gene expression

• Gas exchange 32
• Cell membrane 35
• Enzymes 43
• Genetics 46

Practical section

• Introduction to investigations 63
• Unit 1 Core practical 65

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Transport around the Body
Introduction to circulatory systems
› Living organisms can be classified into organisms that require circulation and organisms that
do not require circulation.
› Small unicellular organisms do not need a transport system, because substances move by
diffusion. This can only occur in unicellular or very small multicellular organisms due to:
• Large surface area to volume ratio.
• Small distance of diffusion.
• Steep concentration gradient.
• Lower energy requirements.
So, there are no limitations of diffusion.
› In larger living organisms, there is a transport system known as the Circulatory system.
› Circulation is either Open or Closed:
• Open circulation: only a heart (hollow muscular tube) is present and there are no blood
vessels.
• Closed circulation: a heart and blood vessels are present (blood is enclosed inside
vessels).
However, there are 2 types of closed circulation:
1. Single Circulation (e.g. in Fish):
• Blood passes by the heart once per cycle.
• Blood is pumped from the heart to the gills for gas exchange (oxygenation) then to
tissues then deoxygenated blood returns back to the heart.
2. Double Circulation (e.g. in Birds and Mammals):
• Blood passes by the heart twice per cycle.
• It consists of
§ Pulmonary circulation: between heart and lungs.
§ Systemic circulation: between heart and body tissues.
› Pulmonary circulation:
Deoxygenated blood is pumped from the right side of the heart to the lungs where oxygenation takes
place. Then, oxygenated blood is returned to the left side of the heart.
• Systemic circulation:
Oxygenated blood is pumped from the left side of the heart to all body tissues. Then, returned back
as deoxygenated blood to the right side.
• Advantages of a double circulation:
1. Complete separation of the deoxygenated and oxygenated blood.
2. The left ventricle pumps blood at a relatively higher pressure for a longer distance to ensure
delivery of oxygen and nutrients to all body tissues.
3. The right ventricle pumps deoxygenated blood at a relatively lower pressure to prevent
damage of the thin and delicate capillaries surrounding alveoli.
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Heart
Site:
Center of the thorax.
Shape:
Inverted cone with base above and apex below, the apex is
pointing to the left.
Size:
About the size of the fist of one hand (300gm).
Supply of Blood:
Coronary arteries (direct branches from the Aorta).
Structure:
› 4 Chambers: right atrium, right ventricle, left atrium and left ventricle.
› 4 Vessels: pulmonary artery, vena cava, pulmonary vein and aorta.
› 4 Valves: right AV valve (tricuspid valve), left AV valve (bicuspid valve), pulmonary SL
valve and aortic SL valve.
› Septum separating the right side from the left side.
Supply of blood: coronary arteries.
Function of the heart (Mass flow)
Transport of substances from high pressure to low pressure over a long distance. This mass transport
helps large multicellular organisms overcome the limitations of diffusion.

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Circulation through the heart:
Use the diagram to describe blood flow through the heart.

1) Deoxygenated blood from the whole body enters the right atrium carried by the vena
cava.
2) Deoxygenated blood is pumped from the right atrium into the right ventricle.
3) Deoxygenated blood is then pumped from the right ventricle to the lungs carried by the
pulmonary artery. In the lungs, oxygenation takes place
4) Oxygenated blood is returned to the left atrium carried by the pulmonary veins.
5) Oxygenated blood is pumped from the left atrium into the left ventricle.
6) The left ventricle pumps oxygenated blood to all the tissues of the body carried by the
aorta.
› Pulmonary circulation: 3 & 4 only
› Systemic circulation: 1 & 6 only

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 Role of Valves:
• They are structures that allow blood flow in one direction and prevent its backflow in
the opposite direction.
• Mechanism of action: a valve opens when pressure before the valve is higher than
pressure after the valve and vice versa.
• A.V. Valves: Allow blood flow from the atria into the ventricles during atrial systole
and prevent backflow during ventricular systole. They are held by Tendons attached to
papillary muscles of the wall of the ventricle to prevent their inversion into atria during
ventricular systole.

• Semilunar Valves: Allow blood from the ventricles into major arteries during
ventricular systole. During diastole, pressure in arteries is slightly higher than
ventricles so blood collects in the pockets closing the valve.

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Cardiac Cycle:
Diastole (0.4s) Atrial systole (0.1s) Ventricular systole (0.3s)
Chamber Both atria and ventricles Atria contracted and Ventricles contracted and
conditions relaxed ventricles relaxed atria relaxed
Pressure Atria is slightly higher Atria is higher than Ventricles is higher than atria
than ventricles ventricles
Valve AV valves open and SL AV valves open and SL AV valves closed and SL
condition valves closed valves closed valves open
Direction Cardiac filling From atria to ventricles From ventricles to major
of blood (Ventricular filling) arteries (Ventricular
flow evacuation)
Volume in 0% to 70% 70% to 100% 100% to 0%
ventricles

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 › Pressure changes during cardiac cycle:

• The lower 2 are bicuspid valves, higher 2 are semilunar valves.

• Label a, b, c, d in a clockwise pattern : Close – Open – Close – Open
• A: Bicuspid valve closes – Pressure in ventricle > Pressure in atrium
• B: Semilunar valve opens – Pressure in ventricle > Pressure in aorta
• C: Semilunar valve closes – Pressure in aorta > Pressure in ventricle
• D: Bicuspid valve opens – Pressure in atrium > Pressure in ventricle
Important Definitions:
› Heart Rate: Number of heart beats per minute.
› Stroke volume: volume of blood pumped in one beat.
› Cardiac output: volume of blood pumped in one minute (HR × SV).
Special Features of the Cardiac Muscle:
› The strongest muscle in the whole body as it is the only muscle that keeps beating throughout
life.
› Can initiate its rhythm through the SAN (Sino-Atrial Node) in the right atrium (Pacemaker).

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Blood Vessels
Artery Vein Capillary

› Narrow lumen. › Wide lumen. › Narrow lumen.

› Thick wall. › Thin wall. › Very thin wall (One cell
› The wall consists of 3 › The wall consists of 3 thick to shorten diffusion
layers: layers: distance)
1) Tunica intima: a single Same as arteries but less › Has capillary pores to
layer of cells developed facilitate exchange of
(endothelium) › Less elastic fibers and substances
2) Tunica media: elastic smooth muscles. › No elastic fibers or
fibres, smooth muscles › Valves present. smooth muscles.
and connective tissue. › Lowest pressure. › No valves.
3) Tunica adventitia: › Pressure is higher than
collagen fibres, smooth veins but lower than
muscles and connective arteries.
tissue.
› More elastic fibers and
smooth muscles.
› No valves.
› Highest pressure.
Role of Elastic Fibers: Factors Ensuring Blood flow Causes of blood pressure
in Veins back to the Heart: reduction in Capillaries:
Ventricular Diastole:
systole: stretch Recoil to 1. Negative pressure in the 1. Leakage of fluids out of
to prevent prevent thorax during inspiration capillaries through
pressure from pressure from causes suction of blood. capillary pores.
becoming too becoming too 2. Muscle pump that pushes 2. Long distance from the
high, so protect low. blood in veins towards the heart.
the artery from heart. 3. Large total surface area
3. Valves prevent backflow of (huge number of
bursting
blood in veins. capillaries).

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Artery:
Adaptations of structure to function:
1) Thick wall to withstand high pressure.
2) Narrow lumen to maintain high pressure.
3) No valves as pressure is too high.

Adaptations of layers to function:

1) Tunica intima:
• Smooth to reduce friction with moving blood.
• Folded to avoid damage when the wall stretches.
2) Tunica media:
• Elastic fibres: they stretch during ventricular systole to prevent pressure from getting
too high and recoil during diastole to prevent pressure from getting too low.
• Smooth muscles: they contract or relax for distribution of blood.
3) Tunica adventitia:
• Collagen fibres: they protect arteries from bursting or external traumas.

N.B If the question is about the adaptations of the aorta, the answer would be the exact same
except for the following points:
1) Relatively large lumen to accommodate the large volume of blood.
2) The aortic semilunar valve is present to prevent backflow of blood during diastole & atrial
systole.

Blood
Blood Constituents
Plasma 55% (Liquid part of the blood) Cells 45% (Solid part)
Water 90% Dissolved substances 10%: RBCs: WBCs: Platelets:
Glucose, salts, minerals, Oxygen Immunity (150000 –
hormones, enzymes, wastes transport 400000/ mm3)
and
Function in
Blood clotting
Plasma proteins (fibrinogen+
albumin+ globulin)

Blood Clotting
› Advantages:
• Prevents loss of health by entry of microorganisms.
• Prevents blood loss.

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 › Mechanism:
• Damaged tissue in the blood vessel wall secretes Thromboplastin protein.
• Platelets are activated by thromboplastin forming a platelet plug that secretes more
Thromboplastin.
• The Coagulation Cascade goes as follows:
1. Thromboplastin converts inactive enzyme Prothrombin into active enzyme
Thrombin.
2. Thrombin converts Fibrinogen (soluble protein) into Fibrin (insoluble protein).
3. Fibrin threads form a mesh trapping blood cells to form a blood clot.
4. This process occurs in the presence of Calcium & Vitamin K.
Important terms:
Energy Budget
It is a term referring to the relationship between energy input & energy output.
Energy input refers mainly to the intake of food & Energy output refers mainly to exercise.

If energy input is higher than energy output this leads to obesity & the opposite causes weight
reduction. This explains why any weight loss program should have two arms: The first arm is
reducing energy intake through having smaller quantities of a balanced diet & the second arm is
increasing energy loss through doing regular exercise

Body Mass Index (BMI)

Obesity (being extremely overweight) is an increasing problem in the Western world. You can
calculate whether or not you are obese by using a formula called the BMI (body mass index). The
formula is shown below.
BMI = Body mass in kg
(Height in m)2

The table shows how BMI values are used to describe the weight of people.

BMI value Description of weight

less than 18.5 Underweight

18.5 to 24.9 Normal weight
25.0 to 29.9 Overweight
30.0 or above Obese

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Cardiovascular Diseases
1. Abnormal Blood Pressure
› Blood pressure is the pressure exerted by blood on the walls of blood vessels.
› It is measured using a Sphygmomanometer.
› Normal blood pressure is about 120/80 mmHg. However, it varies according to:
§ Age
§ Level of activity
§ Position of the person
§ Time of the day
› Hypertension:
A chronic disease characterised by blood pressure reading above 140/90 mmHg sustained and
measured at rest.
› Hypotension:
Sustained blood pressure reading below 90/60 mmHg at rest.
N.B.: To count on a blood pressure reading, it must be sustained (3 successive readings) and at rest.
2. Atherosclerosis
Definition
A disease characterized by thickening and hardening of a
blood vessel (coronary artery) wall as well as narrowing of
the lumen due to the presence of a Fibro-Fatty Plaque.
(Fibro-Fatty Plaques block an artery or increase its chances
of being blocked by a blood clot.)
› Fatty deposits = Atheroma
› If Blood clot formed = Thrombus
Pathology of Atherosclerosis
› Damage of endothelial lining of blood vessels, due to:
• Hypertension.
• Cigarette smoking (Tar).
• Free radicals.
› This stimulates an inflammatory response. WBCs move to the damaged area followed by
accumulation of cholesterol. This is called Atheroma.
› Collagen fibers are then laid down forming a Fibro-Fatty plaque, this causes narrowing of
the blood vessel. This is known as atherosclerosis.
› Atherosclerosis causes hypertension which stimulates further damage (perpetual cycle).
N.B.: Atherosclerosis may stimulate the coagulation cascade causing blood clot formation
(Thrombus).

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Consequences/complications of Atherosclerosis
› Incomplete block of blood vessels → Reduced blood supply (Ischemia) → Angina pectoris.
› Complete block of blood vessels supplying:
§ Heart → Myocardial infarction.
§ Brain → Stroke.
› Weakness of blood vessels → widening at a specific site → Aneurism (which may rupture).
3. Angina Pectoris
› Incomplete block of a blood vessel supplying the heart (coronary artery), causing reduced
blood supply, this lead to anaerobic respiration and lactic acid accumulation.
› Symptoms:
• Sever chest pain during exercise. It is relieved by rest & vasodilators
4. Myocardial Infarction
› Complete block of coronary arteries causing death of the cardiac muscles.
› Explanation:
• Complete obstruction of the lumen of a coronary artery.
• No blood delivered to the cardiac muscle so no oxygen or glucose delivered.
• No aerobic respiration.
• Anaerobic respiration occurs instead.
• Lactic acid is produced from anaerobic respiration.
• This lowers pH
• Enzymes denature.
• Death of the part supplied by the blocked artery
› Symptoms:
• Sudden sever chest pain occurring at rest. It is not relieved by Vasodilators (X angina)
› N.B: The extent of the damage depends on the site and size of the blocked artery. The larger
the size, the greater the damage. This higher the obstruction, the greater the damage. This
occurs as all the area downstream the obstruction is deprived of blood.

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 5. Stroke
› Complete block of a blood vessel supplying the brain (Cerebral artery), causing death of the
part supplied by the blocked vessel.
› Symptoms:
• Vary according to damaged area:
§ Paralysis.
§ Blindness.
§ Loss of speech.
§ Deafness.
6. Aneurysm
› Widening of an artery at the site of atherosclerosis.
› Usually silent (symptomless) but the artery may rupture leading to internal bleeding.

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Risk Factors of Cardiovascular Diseases
Cardiovascular diseases have multiple risk factors (multifactorial). The risk factors are either:
Non-modifiable Risk Factors Modifiable Risk Factors

1. Genetic: It is not a straight forward 1. Smoking: It increases the risk of CVDs

relationship. However, if CVDs are running • Nicotine: Increases adrenaline which
in the family, this increases the risk. increases heart rate and blood pressure.
• CO:
2. Gender: More common in males, it is § Damages endothelium.
thought that estrogen protects females § Forms Carboxyhemoglobin which
against endothelial damage before decreases the O2 delivery to tissues
menopause. But, after menopause, the risk including the heart.
is equal. 2. Diet: Certain types increase CVDs as:
• Cholesterol and LDL
• High levels of salts which causes
3. Age: Elderly are at higher risk mostly due increase in blood pressure.
to damage of elastic fibres, leading to Other types reduce CVDs as:
hypertension. • HDL that remove lipids from tissues.
• Vitamins that act as antioxidants
reducing damage of endothelium.
• Factors that increase the risk of CVD:
§ High total energy input.
§ High cholesterol in diet.
§ Diet with high LDL:HDL ratio.
§ High saturated fats in diet.
§ Diet rich in salts.
§ Alcohol consumption.
§ Caffeine consumption.
3. Exercise: Lack of exercise doubles the
risk. So consequently, regular exercise
can reduce the risk of CVDs to the half
4. Obesity: The risk increases if Waist /
Hip ratio is higher than:
• 0.8-0.9 for females
• 0.9-1.0 for males
5. Stress: Stress leads to high adrenaline
which increases blood pressure.

N.B. Lipids cannot be transported by water. To be transported in blood, they must be coated by LDL
& HDL. HDL is protective as it transports fats from blood to the liver. LDL increases the risk of
CVD as it transports lipids from the liver into blood increasing the risk of atheroma. So to assess
the risk of CVD, we calculate the LDL:HDL ratio. The higher the ratio the higher the risk & vice
versa.

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Treatment of Cardiovascular Diseases
A.Lifestyle modification:
› Quitting smoking
› Reducing total energy input and doing regular exercise.
› Reduce cholesterol in diet.
› Reduce LDL:HDL ratio.
› Avoiding animal fats in diet (Saturated F.A.s) and increase plant oils (Unsaturated F.A.s)
› High vitamins in diet as they act as antioxidants that reduce free radicals lowering the risk
of endothelial damage.
› Reducing or stopping alcohol and caffeine consumption.
› Avoiding stress.
B. Drugs
Drugs
1. Antihypertensives 2. Anticoagulants 3. Statins
Diuretics Vasodilators
Mode of Mode of Mode of Action: They Mode of action: Block the
Action: Action: block certain enzymes in the action of enzymes in the
increase urine widening of coagulation cascade cholesterol synthesis
volume, so blood vessels to reducing blood clotting, so pathway, thus decrease
decreases decrease blood the risk of Cardiovascular cholesterol levels reducing
blood pressure pressure diseases decreases. the risk of atheroma.
Ex.: Thiazides Ex.: ACE Ex.: Low dose Aspirin, Ex.: Atorvastatin.
& Loop inhibitors & B- Warfarin/Heparin
diuretics blockers
Side effects: Side effects: Side effects: May cause Side effects: Constipation,
Hypotension, Hypotension, severe bleeding. Muscle aches, Liver damage
Kidney headache,
problems, dizziness
headache &
dizziness.

4. Others:
› Plant Sterols: They decrease the absorption of fats from the intestine.
› Antioxidants: They decrease free radicals that cause endothelial damage.
C. Surgical methods *read only*
1. Balloon angiography
2. Coronary Bypass
3. Heart Transplantation

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Epidemiology of Cardiovascular Diseases
› Definition:
A branch of medical science that deals with the incidence, distribution and control of diseases in a
population. i.e. it focuses on groups rather than individuals (community-based approach).
› Actual Risk/ Relative Risk:
Probability that a particular event will happen at a given time. Probability is the mathematically
calculated chance of a certain event. This is used to compare with other groups.
› Perceived Risk:
The perceived risk is not always the same as the mathematically calculated risk, it’s the perception
of the community about a certain risk factor. Percentage of a risk depends on: 1. how familiar you
are with this conditions? 2. Do you enjoy it? 3. Do you approve it?
• For Example: The risk of dying from a car accident is 1 in 237 while the risk of dying
from a motorbike accident is 1 in 1020. Yet, people still consider motorbikes more
dangerous than cars.
N.B. Awareness campaigns aim at narrowing the gap between actual risk and perceived risk.
› Very Important Concepts:
Causation: Correlation
› The change in one variable is › The change in one variable is accompanied
responsible for a change in another by a change in another variable.
variable. › Proved by statistical analysis.
› Proved by Laboratory tests. › A similar pattern of change equals a
positive correlation.
› An opposite pattern of change equals a
negative correlation.
› A fluctuating pattern or no change equals
no correlation.

Designing Studies
Types of Studies:
1. Case Control Study
› One group is having the disease (Cases) while the other group is not having the disease
(Control).
› Both groups are asked about the past history of exposure to risk factors.
2. Cohort Study or Longitudinal Study
› Start with normal population and divide into two groups.
› One group is exposed to the risk factor while the other group is not exposed.
› Follow up over a long period of time.

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Evaluating a Study:
A study should be:
1. Repeated: By other who got similar results.
2. Representative sample: Large and random to represent the whole population.
3. Fair: This means that the study is not biased by looking for certain benefits behind the study.
4. Valid: This refers to correct methods &accurate measurements.
N.B. To comment on the validity of the study always look for:
› Sample size: a larger sample size shows variation within the population so it is more
representative.
› Sample selection: controlled variables such as age, gender, level of activity, etc…
› Statistical analysis
› Duration of the study: the longer the duration the better the study (But ONLY in longitudinal
studies)
N.B. Comment on error bars if given
Error bars: they show the spread of data around the mean as they connect the highest value to the
lowest value. The larger the error bar, the lower the reliability & vice versa.

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 Examination Tips

When commenting on graphs, your comment should include description of the trend, pattern
& data manipulation (subtraction, division or percentage change). Don’t make theoretical
assumptions except if you were asked to explain the changes shown by the graph.

When you are asked to calculate the length of the cardiac cycle using pressure / volume
changes table, look for the time between two successive repeated figures. If a graph is given,
look for the distance between two successive peaks on the x-axis.

A cut in blood supply due to blockage of coronary

arteries reduces the delivery of both oxygen and the
respiratory substrate glucose. This stops aerobic
respiration and stimulates anaerobic respiration
which releases lactic acid. Lactic acid reduces pH
which might denature cardiac enzymes causing death
of the cardiac muscle. The extent of damage to the
cardiac muscle depends on the site and size of the
obstructed coronary artery. The higher the level of obstruction in the coronary artery tree, the
greater is the damage, because all the area downstream the occlusion site will be deprived of
oxygen & glucose. Also the larger the size of the artery affected, the greater the damage.

Placebo is a control drug that doesn’t have the active ingredient but looks similar to the real
drug. It could be for example a starch tablet or a water capsule. It is used to compare its effect
with the effect of the real drug and to eliminate the psychological impact of being on a
medication.

To assess the correlation between a risk factor and a disease using 2 graphs, look for the
pattern of change. If the pattern of the risk factor graph obeys and precedes the disease graph,
this suggests a correlation. A fluctuating or opposing pattern never suggests a correlation.

Morbidity = disease presence, Mortality = Death from the disease. Differences in morbidity
or mortality rates in different populations are usually attributed to differences in health
education & awareness, the presence of new medications, the presence of different risk factors
& sticking to protective measures.

Morbidity and mortality rates are calculated as a number per 100,000 as population sizes are
different so this allows for a valid comparison.

Biological Molecules
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 › Types of bonds:
1. Hydrogen bonds: weak bonds between slightly charged atoms.
2. Ionic bonds: strong bonds between strongly charged ions.
3. Disulfide bridges

› Molecules are either polar or non-polar:

1. Non-polar: there’s an even distribution of charges.
2. Polar: there’s an uneven distribution of charges.
Polar molecules are either unipolar or dipolar.

Water (H2O)
› Water molecules are non-linear and dipolar due to different sizes of atoms and
uneven distribution of charges.
› Water has a dipolar nature due to uneven distribution of charges. This allows
the formation of hydrogen bonds with all polar particles. Positive ions bond
with the negative end of water while negative ions bond with the positive end
of water. So all polar structures dissolve in water. This makes water an
excellent solvent.
› Moreover, water molecules can form hydrogen bonds with each other (cohesion) as well as
with nearby surfaces (adhesion). This allows water to move as one unbroken column.
› An excellent solvent that moves as one unbroken column is definitely a perfect transport
medium.
Water Properties
1. Excellent Solvent.
2. Amphoteric:
Keeps constant pH as it acts as a proton donor or a proton acceptor. So, it acts as a buffer during
metabolic reactions.
3. Transparent:
Allows marine life to exist due to passage of sunlight and photosynthesis.
4. Low Density:
Ice floats on the surface insulating the lower water which allows for the continuity of marine life.
5. High specific heat capacity (SHC):
Keeps water temperature within narrow limits. This allows for proper enzyme activity of aquatic
organisms.

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Organic Molecules
Important Definitions
› Molecular Formula: Number of each type of atom in a molecule. Ex.
Glucose C6H12O6
› Structural Formula: Arrangement of atoms in a molecule. Ex. Ring form
› Monomers: Also called subunits or residues, they can be bonded together
by condensation reactions to form larger molecules.
› Isomers: Are molecules having the same molecular
formula but different structural formulae. Example:
α Glucose & B glucose (both C6H12O6 )
› Macromolecule: Large molecule formed of many
subunits called “Monomers”.
› Polymer: Macromolecule made of identical
monomers.
› Condensation: Removing water to join two molecules forming a larger one.
› Hydrolysis: Adding water to breakdown a large molecule into smaller ones.
N.B. All polymers are macromolecules, but not all macromolecules are polymers. For example,
polypeptides and polysaccharides are polymers, while lipids are macromolecules but not polymers
as their subunits are not identical (fatty acids & glycerol)

Carbohydrates (CH2O)n
Monosaccharaides
Monomers of Carbohydrates
› They could be either:
• Trioses: Only three carbon atoms C3H6O3
• Pentoses: Only five carbon atoms C5H10O5
• Hexoses: Six carbon atoms C6H12O6
› Hexoses include Glucose, Galactose and Fructose

All down except 3 up All up except 2 down

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 › Glucose structure:

How to draw a-glucose:

1) Draw an empty ring.
2) Draw carbon number 6.
3) Add your OHs (All down except 3 up).
4) Add your missing Hs.
Disaccharides
Two monomers joined together.
› They could be either:
• Maltose: 2 α-Glucose molecules →
• Sucrose: α-Glucose + Fructose.
• Lactose: α-Glucose + Galactose.
› Monomers are joined by condensation reaction (joining two molecules by removing water)
and broken by hydrolysis (breaking two molecules by adding water)

Glucose & Galactose monomers joined by condensation forming Lactose

› The bond joining α-Glucose molecules is α 1-4 glycosidic bond.

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Properties of Monosaccharides and Disaccharides
1) Small/Low molecular weight.
2) Soluble in water/polar/hydrophilic.
3) Sweet in taste.
Polysaccharides (Large number of monomers joined by condensation)
Starch (formed of) Glycogen
Amylose 30% Amylopectin 70% › Similar to
Amylopectin but
› Unbranched chain of α- › Branched chain of α-Glucose branches are more
Glucose joined by α 1,4- joined by α 1-4 glycosidic frequent (every 10
glycosidic bonds. bonds. glucose subunits).
› Coiled into helix. › Branches arise every 20-30
glucose subunits by α 1-6
glycosidic bonds at the
branching point

Starch:
› It’s a polymer of a-glucose monomers joined together by a 1,4 glycosidic bonds formed
through condensation reactions.
Properties of Polysaccharides
1) Large/high molecular weight.
2) Insoluble in water/non-polar/hydrophobic.
3) Non-sweet in taste.

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Summary for Carbohydrates Classification
1. Monosaccharaides: Single sugar units (low molecular weight, sweet taste, soluble in water)
• Glucose: used in respiration.
• Fructose: found in fruits.
• Galactose: forms lactose of milk.
2. Disaccharides: 2 sugar units
• Maltose: 2 α-Glucose molecules.
• Sucrose: Glucose + Fructose.
• Lactose: Glucose + Galactose.
3. Oligosaccharides: 3-10 sugar units, found in vegetables as beans.
4. Polysaccharides: long chains of glucose (high molecular weight, tasteless & insoluble)
• Starch: storage in plants.
• Glycogen: storage in animals.
Adaptations of Starch and Glycogen for their Storage Function *Very important*
1. Large molecules: to store a lot of energy.
2. Compact: to store a large number of glucose molecules while occupying less space.
3. Insoluble: doesn’t affect osmotic pressure.
4. Non-reactive: doesn’t interfere with any metabolic reactions in the cells.
5. Rapidly hydrolyzed by enzymes: as the a 1,6 glycosidic bond is easily broken down.
N.B. General formulae:
- Monosaccharides: CnH2nOn
-Disaccharides: CnH2n-2On-1
-Polysaccharides: Cx(H2O)Y

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Lipids
› They are formed of C, H & O like carbohydrates but the ratio of H:O is not 2:1
› The most common form is Triglycerides
Triglycerides
§ Energy supply.
§ Energy storage.
§ Thermal insulator.
§ Electrical insulator.
§ Buoyancy.
§ Supporting many organs.
› Formed of 1 Glycerol and 3 Fatty acids.

› As shown above, Triglycerides are formed of glycerol head and 3 Fatty acid tails joined by
condensation forming Ester Bond.
Types of Fatty acids
Saturated Fatty acids Unsaturated Fatty acids
› FA chain contains the maximum possible › FA chains contains less than the maximum
number of H-atoms. (saturated with number of H-atoms.
hydrogen) › C=C double bonds (1=MUFA, if ˃1
› No C=C double bonds =PUFA)
› Straight structure › Kinky structure
› Example: animal fat › Example: plant oils.
› Causes CVDs. › Don’t cause CVDs.
› High melting point › Low melting point

N.B. Saturated fats are tightly packed so they have strong intermolecular forces and a high level of
heat energy is needed to break these forces unlike unsaturated fats which are loosely packed.
N.B. The general formula of saturated fatty acids is CnH2nO2
© Dr. Mohab Megahed 25
Phospholipids
› Same as Triglycerides, but one of the FAs attached to glycerol is replaced by phosphate
group.
› Formed of a polar hydrophilic head (phosphate group) and 2
non-polar hydrophobic tails (fatty acids).
› Form an important part of cell membrane, the Phospholipid
Bilayer.

N.B. All fats are hydrophobic

N.B. Since fats are hydrophobic, they cannot dissolve in the water of plasma. To be transported in
blood, fats must be coated by proteins (hydrophilic), forming lipoproteins.
Cholesterol
› Short lipid molecule with a structure different to Triglycerides.
› Important part of Cell membrane (between phospholipids), Sex hormones and Bile salts

© Dr. Mohab Megahed 26

Proteins
› They are formed of C, H, O and N (± phosphate and sulfur).
› They are polymers of Amino acids formed by condensation reaction.
Amino Acids

› All amino acids have the same backbone consisting of a central carbon attached to H, carboxyl
group on one side and amino group on the other side as well as a variable R group.
› There are only 20 types of AAs. However, by using different numbers, sequences and
combinations a huge number of proteins can be produced.
› Humans can only make 12 AAs in their bodies. The others must be supplied in diet, so they
are called essential Amino acids.
Peptide Bond Formation

› One Amino acid loses OH from the Carboxylic group, the other Amino acid loses H from
the Amino group (Condensation reaction).
› The bond is broken by addition of H2O (Hydrolysis reaction).
› The backbones of all Amino acids are similar, the only thing that differentiates between
them are the R-groups. So, the R-groups:
§ Determine the properties of the Amino acid.
§ Determine the function of formed proteins.
§ Determine types of bonds that hold proteins in the 3ry and 4ry structures.

© Dr. Mohab Megahed 27

Levels of Protein Structure
Primary Structure:
The number, type and sequence of Amino acids in the polypeptide chain. Held by peptide bonds.

Secondary Structure:
Slight bending of the polypeptide chain producing α-helix or β-pleated sheets. Formed between
slightly charged atoms in the backbone of amino acids (Hydrogen bonds).
• R-groups are not involved in the 2ry structure.
• Backbones are similar, so the 2ry structure is not specific for particular proteins.
α-helix β-pleated sheets
Formed by H-bonds between amino acids of one H-bonds between amino acids of one chain
turn and those of the next turn. Ex. Keratin of and amino acids of an adjacent chain. Ex.
nails and skin. Fibroin in silk protein.

Tertiary Structure:
The bending and folding of the polypeptide chain into a precise, complex and unique 3D shape
through the formation of bonds between R-groups. The bonds are of the following types:
1. Hydrogen bonds 2. Ionic bonds 3. Disulfide bonds
› Formed between the small › Formed between the charged › Formed between R-groups
+ve charge of the Hδ+ and amino group and charged of amino acids that contain
the small –ve charge of the carboxyl group of R-groups sulfur.
δ-
O found on R-groups. of the amino acid. › The strongest of the three
› Very weak bonds, › Stronger than H bonds but types of bonds.
› Broken by temperature weaker than disulfide bonds. › Only broken by reducing
› Broken by PH agents.
4. Hydrophobic interactions: they are not real bonds, but the presence of hydrophobic R-
groups makes the polypeptide chain bend or fold.

© Dr. Mohab Megahed 28

Quaternary structure:
More than one polypeptide chain linked together to form a complex functioning protein. Such as
Insulin hormone (2 chains) and Hemoglobin (4 chains).
Chains are linked by the same types of bonds of the Tertiary structure.
N.B. Conjugated proteins: Proteins having a non-protein part called prosthetic group, such as:
Glycoproteins, Lipoproteins and haemoglobin.

› Comparison between globular and fibrous proteins:

Points of Comparison Globular Fibrous
Structure 3ry structure and sometimes 2ry structure and sometimes
4ry. Held by hydrogen, ionic 3ry. Held by hydrogen bonds
bonds, disulfide bridges between the backbones.
between R groups.
Shape Ball shaped Long parallel fibers

Specifity Specific Non-specific

Solubility Insoluble Soluble
Function Metabolic functions Structural functions
Examples Enzymes and Hormones Keratin in skin and nails.
Fibroin in silk.

© Dr. Mohab Megahed 29

Denaturation of Proteins
Loss of the complex precise 3D shape leading to loss of the function (Loss of tertiary structure).
› Causes:
1. Very high temperature: breaks H-
bonds only.
2. Major changes in pH: breaks H-bonds
and ionic bonds.
3. Reducing agents: break disulfide
bonds.

Examination tip
Describe how the 1ry structure determines the 3ry structure & properties of an enzyme?
The primary structure determines the type, number & sequence of AAs in the polypeptide chain
so it determines the arrangement of the R groups and consequently the bonds to be formed
between those are groups such as Hydrogen bonds, ionic bonds or disulfide bridges.
Those bonds are responsible for bending & folding of the polypeptide chain to arrive at a precise
3ry structure with a specific shape of the active site (complementary to a certain substrate) leading
to enzyme specificity.
Moreover, the intact primary structure guarantees that the 3ry structure will have proper
positioning of the hydrophilic R groups outwards and hydrophobic R groups inwards ensuring
enzyme solubility.

© Dr. Mohab Megahed 30

© Dr. Mohab Megahed 31
Gas Exchange
› Gas exchange in lungs: entry of oxygen in blood & exit of carbon dioxide from blood by
diffusion.
› Gas exchange in tissues: entry of carbon dioxide in blood & exit of oxygen from blood by
diffusion.

Fick’s law of diffusion

Any gas exchange/diffusion surface should have:

1) Large surface area.
2) Steep concentration gradient.
3) Short diffusion distance.

Ventilation (Breathing)
It is the movement of air in (inspiration) and out of the lungs (expiration).
Ventilation is controlled by two groups of muscles: The Diaphragm and Intercostal muscles.
Inspiration Expiration

1. Diaphragm: contracts and flattens. 1. Diaphragm: relaxes & domes.

2. Intercostal muscles: contract 2. Intercostal muscles: relax
3. Rib cage: raised upwards & outwards. 3. Rib cage: drops down.
4. Volume of thorax: increases. 4. Volume of thorax: decreases.
5. Pressure inside: Decreases below 5. Pressure inside: increased above
atmospheric pressure. atmospheric pressure.

© Dr. Mohab Megahed 32

Examination tips:
Role of the circulatory system in gas exchange:
The heart generates mass flow, which is pumping blood from higher pressure to lower
pressure over a long distance. This ensures delivery of deoxygenated blood to the lungs and
oxygenated blood to all other tissues, which maintains concentration gradients.
Capillaries are the sites of gas exchange to which they are adapted by:
1) Large total surface area to increase the rate of diffusion.
2) Very thin walls to shorten diffusion distance.
3) Capillary pores to facilitate exchange of substances.
All the above helps to overcome limitations of diffusion (such as…)
If you are asked about importance of the heart for gas exchange, Describe mass flow only. If
you are asked about importance the whole circulatory system discuss mass flow + importance
of capillaries. (as shown in the previous tip)

Alveoli:
› They are the tiny air sacs where gas exchange takes place.

Examination tips:
Remember that any gas exchange surface must have the following features to ease diffusion
of gases: Large surface area to volume ratio, Steep concentration gradient & thin surface
membranes.
The role of the respiratory system in gas exchange:
Ventilation maintains concentration gradient (as it brings inhaled air rich in O2 and removes
exhaled air rich in CO2.
Alveoli are responsible for gas exchange to which they are adapted by:
1. Large total surface area: as surface area is proportionate to diffusion.
2. Surrounded by a rich network of blood capillaries
3. Very thin wall (one cell thick) to shorten diffusion distance
4. Lined by a layer of moisture to prevent drying out of cells
All the above helps to overcome limitations of diffusion (such as…)

© Dr. Mohab Megahed 33

Oxygen dissociation curve:

Oxygen dissociation curve

100
Percentage oxygen saturation of

90
80
70
Haemoglobin/%

60
50
40
30
20
10
0
0 20 40 60 80 100
Partial pressure of oxygen/mmHg

Presence of CO2 Normal Haemoglobin Fetal haemoglobin

It’s a sigmoid-shaped curve showing partial pressure of oxygen on the X-axis and
percentage oxygen saturation of Haemoglobin on the Y-axis.

This graph shows that Haemoglobin has low affinity to oxygen in tissues with low partial
pressure of oxygen (For example: exercising muscles) while Haemoglobin has high affinity
to oxygen in tissues with high partial pressure of oxygen (For example: lungs).

The above explains how Haemoglobin transports oxygen in our bodies as it binds to oxygen
in the lungs and leaves this oxygen in the tissues.

The Bohr effect: the presence of carbon dioxide reduces the percentage saturation at all
partial pressures. This means that Haemoglobin has a lower affinity to oxygen in tissues
with high carbon dioxide concentration or low pH so the graph shifts to the right.

Fetal Haemoglobin: Fetal Haemoglobin has higher affinity to oxygen than the normal adult
Haemoglobin. This leads to shifting of the oxygen dissociation curve to the left. This is due
to the different chemical structure from adult Haemoglobin. However, 6 months after birth
all fetal Haemoglobin is replaced by normal adult Haemoglobin.

© Dr. Mohab Megahed 34

Cell Membrane
Structure:
› Thickness → about 7 nm.
› Components:
• Lipids
§ Phospholipids (in the bilayer)
§ Cholesterol (inbetween phospholipid tails)
• Proteins
§ Intrinsic proteins (spanning the full thickness of the cell membrane)
§ Extrinsic proteins (found in one layer only)
• Carbohydrates
§ Glycoproteins
§ Glycolipids

Fluid Mosaic model of the Cell Membrane

› Fluid: Phospholipids are in continuous motion within their monolayer, exchanging places and
pumping into each other.
› Mosaic: This term refers to the random distribution of proteins among the phospholipid
bilayer.
N.B. The Davson-Danielli model: 2 hydrophilic protein layers with a phospholipid bilayer in
between.

© Dr. Mohab Megahed 35

 A. Membrane Lipids
› Phospholipids
§ Hydrophilic head (Phosphate).
§ Hydrophobic Tails (2 Fatty acids).
• N.B.: Orientation: They form a bilayer with hydrophilic
phosphate heads facing outwards and inwards to form hydrogen
bonds with two aqueous media (Extracellular fluid outside the
cell and cytoplasm inside the cell) while the hydrophobic tails are facing each other in
the centre of the bilayer held together by hydrophobic interactions.

• Importance of Phospholipids (Functions):

1. Form the structural framework of the cell membrane (a barrier between two aqueous media)
2. Responsible for the fluidity of the cell membrane.
Fluidity is increased by:
§ Increase of unsaturated Fatty acids. If the fatty acids are mostly unsaturated
they kink easily, which increases fluidity.

§ Increase in temperature.
§ Decrease in cholesterol.

3. Responsible for selective permeability, they allow diffusion of:

a. Small polar molecules as water.
b. Non-polar lipid soluble molecules.
c. Gases as O2 and CO2

© Dr. Mohab Megahed 36

 › Cholesterol:
• It consists of a Hydrophilic head and a hydrophobic tail, its
structure helps it fit between phospholipids molecules.
• They are held together by hydrophobic interactions.
• Importance:
1. Regulates cell membrane fluidity.
2. Provides mechanical (structural) stability.
B. Membrane proteins
› They are globular proteins with hydrophilic R-groups facing outwards and inwards while
hydrophobic R-groups are in the center towards fatty acid tails and held in place by
hydrophobic interactions.
› They could be either embedded in one layer (Extrinsic proteins) or occupying the full
thickness of cell membranes (Intrinsic proteins).
› Importance:
1. Channel proteins: Intrinsic proteins that form hydrophilic tunnels among the hydrophobic
center of the bilayer. They are either:
§ Permanently open: rapid movement of water.
§ Gated channels: may open or close.
They help in facilitated diffusion.
2. Carrier proteins: Specific proteins that bind to specific molecules. They help in facilitated
diffusion and active transport.
3. Enzymatic proteins: Catalyze important reactions.
C. Membrane Carbohydrates
› They are either:
• Glycoproteins
a) Recognition proteins: Also known as antigens.
b) Receptor proteins: Bind with specific molecules to trigger certain reactions inside
the cell.
• Glycolipids
› They also stabilize the cell membrane by forming H-bonds with water.

© Dr. Mohab Megahed 37

Transport across Cell Membrane
A. Simple Diffusion
› Definition:
Passive movement of substances down concentration gradient through the phospholipid bilayer such
as:
i. Gases
ii. Water (Despite being dipolar; it’s small enough to pass in-between the hydrophobic
tails of the phospholipid bilayer)
iii. Non-polar lipid soluble substances such as ethanol & glycerol
N.B Increasing fluidity increases the movement of substances by simple diffusion leading to
higher membrane permeability.

B. Facilitated Diffusion
› Definition:
Passive movement of substances down concentration gradient through channel proteins.
Channel proteins form hydrophilic tunnels through the hydrophobic centre of the bilayer,
allowing for the passage of large polar structures such as:
i. Glucose
ii. Amino acids
N.B Factors affecting Diffusion:
Both are called
1. Steepness of the concentration gradient.
Electrochemical gradient
2. Electric gradient: Ions attached to opposite charge.
3. Temperature: Increasing temperature increases diffusion.
4. Surface area: Increasing surface area increases diffusion.
5. Thickness of the membrane.
6. Size of the molecules: Smaller diffuses faster.
7. Polarity of the molecules: Non-polar molecules diffuses faster.
N.B Osmosis:
› Definition:
The net movement of water down water potential gradient through a partially permeable membrane.
› Water molecules can pass through one of the two pathways:
a) Inbetween phospholipids (Simple diffusion)
b) Through channel proteins (Facilitated diffusion)
› Water potential is a measure of the tendency of water to move from one place to another due
to its kinetic energy. Pure water has the highest water potential which is zero.
› Factors affecting Osmosis:
• All factors of Diffusion in addition to:
1. Solute concentration: adding solute to pure water restricts the movement of water
molecules.
2. Pressure applied to water: The higher pressure applied, the higher the water potential.

© Dr. Mohab Megahed 38

 C. Active Transport
› Definition:
The movement of molecules from low concentration to high concentration through a living
membrane i.e. against concentration gradient. It needs energy (ATP) and carrier proteins.
› Types of Carrier Proteins:
• Pass one kind of molecules/ions inside or outside.
• Pass one ion in and one out like the Na+ - K+ pump.
• Pass two molecules at the same time as Na+ and glucose (Sodium Co-transport).
› Mechanism of Active Transport:
• A certain molecule or ion binds to a receptor on
the surface of a specific carrier protein.
• ATP inside the cell is broken down by ATPase
enzyme releasing ADP and Pi. Pi binds to the
carrier protein.
• Phosphate causes the protein carriers to change its
shape by Swinging Doors or Rotation
Mechanisms.
• Phosphate detaches and the carrier restores its
original shape.

› What are the evidences for Active Transport?

• Occurs only in living cells.
• More in cells with more mitochondria.
• Respiratory poisons as cyanides stop active transport.
› Factors affecting Active Transport:
1. Oxygen concentration, since aerobic respiration provides ATP
2. Number of carriers
3. Number of mitochondria in the cell to provide ATP
4. Presence of respiratory poisons as cyanide.

© Dr. Mohab Megahed 39

 D. Cytosis (Bulk transport)
› Definition:
Transport of large bulks of materials across the cell membrane using vacuoles or vesicles.
• It is an active process that requires energy.
• It is either Endocytosis or Exocytosis.
› Endocytosis:
Taking material inside the cell actively using vacuoles.
Phagocytosis Pinocytosis
Bulk transport of solids actively. Bulk transport of liquids.
Ex.: phagocytes engulfing bacteria. Ex.: Ovum taking nutrition.
› Exocytosis:
Removing materials outside the cell actively by emptying vacuoles.
• The opposite of endocytosis.
• Vesicles fuse with the cell membrane
releasing their secretions outside. These
vesicles are guided by microtubules.
• Example:
§ Secretion of mucus by goblet
cells.
§ Secretion of pancreatic amylase

© Dr. Mohab Megahed 40

Graph showing diffusion & active transport

Diffusion

Concentration of substance
X inside the cell

Time

› First region: steepest increase in the concentration of substance X inside the cell.
Explanation: Highest concentration gradient so highest rate of diffusion.
› Second region: less steep increase in the concentration of substance X inside the cell.
Explanation: Lower concentration gradient so lower rate of diffusion.
› Last region: No change in concentration of substance X inside the cell.
Explanation: Equilibrium is achieved so diffusion stops.

N.B. Active transport graph shows a linear change as it’s not affected by concentration gradient.

Active transport
Concentration of substance
X inside the cell

Time

© Dr. Mohab Megahed 41

Graph showing effect of temperature on diffusion

Concentration of substance X
inside the cell

Temperature

› First region: Increasing temperature increases concentration inside the cell.

Explanation: Higher kinetic energy so higher rate of diffusion.
› Second region: Marked increase in concentration of substance X inside the cell.
Explanation: Very high temperature leads to melting of the phospholipid bilayer and
coagulation of membrane proteins. This damage to the cell membrane ends by loss of
selectivity and marked increase in permeability.
› Last region: No change in concentration of substance X inside the cell.
Explanation: Equilibrium is achieved so diffusion stops.
N.B. High concentrations of ethanol dissolve the phospholipid bilayer leading to cell membrane
damage. This damage ends by loss of selectivity and marked increase in permeability.

Membrane fusion trial

› Proteins of a certain membrane were labelled with green colour.
› Proteins of another membrane were labelled with red colour.
› When we fused the membranes, the following occurred:
1) A single membrane was produced with the same total number of proteins (Fluid)
2) Red and green proteins were scattered randomly in the fused membrane (Mosaic)

© Dr. Mohab Megahed 42

Enzymes
Definition:
› They are biological catalysts.
Biological: as they are proteins formed inside the cell.
Catalysts: as they speed up the rate of reactions without being used up or changed.
Characteristics
› They are proteins in nature. Globular proteins with hydrophilic R-groups outside and
hydrophobic inwards which ensures solubility of the enzyme.
› Most enzymes are specific. However, some enzymes are not very specific such as Trypsin
which works on many proteins.
› Each enzyme is formed of an active site and body. The active site fits with the shape of the
substrate, it is a cleft formed of 3-12 amino acids.
› The rest of the enzyme (Body) provides structural stability.
Enzymes Catalyze Two Types of Reactions
Anabolic Catabolic
› Building large molecules from smaller › Breaking large molecules into smaller
ones. Endothermic, Endergonic ones. Exothermic, Exergonic
Mechanism of Action
› All enzymes work by reducing the Activation Energy
(EA). This is the energy required to get the reaction to
start. This occurs as collisions between the enzyme
molecule and the substrate weaken bonds in the
substrate.
› Enzymes provide an alternative reaction pathway inside
the active site which requires less energy to start.
Specifity
› Enzymes bind their substrate at the active site using
one of two mechanisms.
§ Key and Lock mechanism.
§ Induced Fit mechanism.

© Dr. Mohab Megahed 43

 › Lock and Key Mechanism:
• The shape of the active site is complementary to the shape
of the substrate exactly (Enzyme specificity).
• The Enzyme-Substrate complex is held by H-bonds
temporarily.
› Induced Fit Mechanism:
• The shape of the active site is not exactly complementary
to the shape of the substrate.
• When the substrate enters the active site, small changes
occur in the active site resulting in a perfect fit. i.e. the
substrate entrance induces the fitting as the active site
molds around the substrate.
Factors affecting Enzyme Activity

1. Temperature:
- A rise in temperature increases the rate of a chemical
reaction because both the enzyme and substrate gain
kinetic energy which increases the frequency of
successful collisions leading to a greater number of
enzyme substrate complexes. This continues until the
optimum temperature is reached at which the highest
rate of reaction occurs.
- Further increase beyond the optimum temperature, the
rate of reaction drops rapidly until it completely stops
due to denaturation of the enzyme.
Denaturation means that the shape of the enzyme’s
active site changes permnantly as temperature breaks
Hydrogen bonds and thus it no more fits the substrate.

- At temperature 0 enzymes and substrates are frozen and there is no kinetic energy for
movement. This is a state of reversible deactivation.

© Dr. Mohab Megahed 44

 2. pH:
- pH scale runs from 1 to 14. Neutral PH is 7, below this is
acidic and above this is alkaline.
- Each enzyme has its optimum pH at which the highest rate
of reaction takes place.
- Minor changes above or below the optimum pH reduce the
rate of reaction.
- Major changes from the optimum pH denature enzymes.
This could be explained by the ability of pH changes to
break ionic bonds between amino acids forming the active
site so it can no more fit its substrate which leads to denaturation
of the enzyme.

3. Enzyme/Substrate concentration: Increasing enzyme

concentration increases the rate of reaction as it increases the
availability of active sites which consequently increases the
chances of successful collisions. This continues until there is no
more substrate available so it levels off. (The same occurs when
we increase the substrate concentration)
How can we measure the rate of Enzyme controlled reactions?
› Either by: Determining the quantity of substrate used up or the quantity of product given
out.
› This should be done at the initial phase (V0) or rapid phase where there is still a plenty of
the substrate & the substrate is not yet a limiting factor so the reaction mainly depends on
enzyme concentration. (i.e. it should be done before reaching Vmax)
N.B Why do we prefer measuring the initial rate of reaction?
As there is plenty of substrate molecules available, so the maximum chances of successful
collisions occur, and the highest possible rate of reaction is achieved (Substrate concentration is
not a limiting factor yet).

© Dr. Mohab Megahed 45

Genetics
Some Important Definitions
› Gene:
Short length of DNA coding for a certain characteristic through protein synthesis.
› Alleles:
Alternative forms of the same gene. Where one may be dominant and the other may be recessive.
› Dominant Allele:
An allele that can show itself on the phenotype in the presence or absence of the recessive one (B).
Expressed if the genotype is homozygous dominant or heterozygous.
› Recessive Allele:
An allele that can only show itself on the phenotype in the absence of the dominant allele (b).
Only expressed if the genotype is homozygous recessive.
› Heterozygous:
A person having two different alleles for one gene, one is dominant and the other is recessive.
› Homozygous:
A person with two similar alleles for the same gene, both dominant or both recessive.
› Genotype:
The alleles of a certain genes. (Bb)
› Phenotype:
External appearance of a certain individual as a result of interaction between the genotype and
environment.
› Diploid vs. Haploid:
• Diploid: Two of each kind of chromosome, 2n or full set.
• Haploid: One of each chromosome, 1n or half set.
N.B.: Revise genetic diagrams from your O-level. Then use the family pedigree below to state
which of the family members must be carriers of cystic fibrosis (CF is a recessive inherited disorder)

© Dr. Mohab Megahed 46

Nucleic Acids (DNA & RNA)
› Nucleic acids are formed of many nucleotides joined together so they are called
polynucleotides.
A Nucleotide is formed of
› Pentose sugar:
• Ribose for RNA
• Deoxyribose for DNA
› Nitrogenous base attached at C1 of the sugar, they are either:
• Purines (2 rings)
§ Adenine (A).
§ Guanine (G).
• Pyrimidines: (1 ring)
§ Cytosine (C).
§ Thymine (T).
§ Uracil (U) → instead of thymine in RNA
› Phosphate group (-vely charged) attached to C5 of the sugar.

Polynucleotide chain
› Consists of many DNA nucleotides held together by
phosphodiester bonds between phosphate attached to C5 of
one nucleotide & C3 of the next nucleotide forming the
Sugar-Phosphate Backbone.
› This covalent bond is formed by a condensation reaction with
loss of H2O molecule.
› The polynucleotide chain has 2 ends; 3’ end and 5’ end.

© Dr. Mohab Megahed 47

Structure of DNA

› Consists of 2 DNA strands (2 polynucleotide chains) running antiparallel with the 5’ end
facing the 3’ end of the other strand.
› The two strands are held together by H-bonds between nitrogenous bases according to
complimentary base pairing rules.
• A=T
• G≡C
› Explanation:
• The space between backbones is just enough for 3 rings (Purines have 2 rings and
Pyrimidines have 1 ring).
• Both A and T have 2 weak charges so they form 2 hydrogen bonds.
• Both C and G have 3 weak charges so they form 3 hydrogen bonds.
(A needs 2 H-bonds just as T, while G needs 3 H-bonds just as C.)
› The two strands (polynucleotide chains) are coiled around each other forming a double
helix.
› DNA is a perfect genetic material:
1. Can carry instructions for protein synthesis.
2. Stable structure.
3. Can replicate easily and perfectly.

© Dr. Mohab Megahed 48

DNA Replication (Semiconservative replication)

Now after understanding the process, check this

diagram for further elaboration of the concept of
semiconservative replication →
N.B Why is DNA replication described as
semiconservative replication?
Each daughter molecule is half old (1 strand from
the parent) and half new (1 newly formed strand).

© Dr. Mohab Megahed 49

Evidence that DNA-replication is Semi-conservative (Meselson and Stahl experiment)

1. Grow E. coli cells in a medium with N15 as a sole source of nitrogen, collect a sample and
purify DNA.
2. Transfer cells to a medium containing N14. Leave them to divide once, then collect a sample
and purify DNA.
3. Leave cells to divide a second time then collect a sample of DNA and purify.
4. Centrifuge the 3 samples and compare the location of the DNA bands, DNA containing N15
is heavier and forms a lower band.
› Explanation:
• Original DNA was all heavy N15
• 1st generation has half-old (N15) and half-new (N14) → hybrid middle band.
• 2nd generation has two bands, one hybrid band in the middle and one light (N14) higher
band.
› Question:
Now draw the 3rd generation and its centrifuged band on the blank page.

© Dr. Mohab Megahed 50

RNA
› Structure
• Single stranded polynucleotide molecule.
• Each RNA nucleotide:
§ Pentose Sugar: Ribose
§ Nitrogenous Base: Adenine, Uracil (No Thymine), Cytosine and Guanine.
§ Phosphate group.
• RNA molecules could be found inside the nucleus or the cytoplasm, unlike DNA which
is only found in the nucleus.
• RNA cannot replicate like DNA, it is also less stable.
› Types of RNA:
• Messenger RNA (mRNA).

• Transfer RNA (tRNA).

• Ribosomal RNA (rRNA).

© Dr. Mohab Megahed 51

Genetic Code
› Definition:
Three successive nitrogenous bases on the antisense strand of DNA coding for the placement of
a certain amino acid on the polypeptide chain.
› Characteristics:
• Triplet: Each amino acid is coded for by three successive bases (43= 64 possible
combinations). If singlet: 41= 4 codes only. If doublets: 42= 16 codes only.
• Degenerate: There are 64 possible codes, each amino acid may have more than one
code, but a single code can’t give more than one amino acid.
• Universal: Amino acids have same codes in almost all living organisms.
• Non overlapping: No base in a certain triplet code is used by an adjacent triplet code.

Protein Synthesis
Intro:
› Each chromosome is a molecule of DNA.
› A gene is a short length of DNA coding for synthesis of a certain protein.
› The gene consists of many genetic codes.
Overview:
› Protein synthesis consists of Transcription and Translation
› Transcription: formation of mRNA from the gene in the nucleus.
› Translation: formation of a polypeptide chain using mRNA & tRNA in the cytoplasm.
1. Transcription
› Definition:
The process by which the base sequence on one strand of DNA molecule
(called the antisense strand) is converted into a complementary base
sequence forming messenger RNA, it occurs in the nucleus catalyzed by
RNA polymerase enzyme.
› Steps:
› A specific length of DNA (gene) unwinds & unzips. This is
catalyzed by DNA helicase enzyme. One of the two strands will
be used as a template for mRNA formation (Antisense strand)
while the other strand remains inactive.
› The antisense strand attracts free active RNA nucleotides according to complementary base
pairing rules T=A, A=U and G≡C. Then, RNA-polymerase enzyme catalyzes the formation
of hydrogen bonds and phosphodiester bonds (joins the sugar-phosphate backbone).
› Now, a single stranded mRNA is formed, it detaches and leaves through nuclear pores heading
to the ribosome.
› RNA-polymerase detaches, DNA strands rejoin each other to form a double helix again.

Now: every three bases on mRNA strand are called Codons as they code for a specific amino
acid on the polypeptide chain.

© Dr. Mohab Megahed 52

 2. Amino Acid Activation
› There are 20 amino acids, each amino acid has a specific tRNA to
carry it. So, consequently we have 20 tRNA types.
› Each tRNA is clover shaped. It has an anticodon formed of 3
nitrogenous bases complementary to those of mRNA on one side and
amino acid binding site on the other side.
› Amino acid activation is the binding of amino acids to their specific
tRNA in preparation for the 3rd phase of protein synthesis
(Translation).
3. Translation
› Definition:
The process by which the ribosome reads mRNA sequence and translates it into the amino acid
sequence on the polypeptide chain.
› Steps:
1. mRNA binds in the cleft between the two subunits of the ribosome. This space can only
accommodate 2 codons at one time (6 bases).
2. The first codon on all mRNA molecules is AUG which codes for Methionine (start codon/
initiation codon).
3. Two tRNA molecules bind to mRNA as their anticodons are complementary to mRNA
codons so they form H-bonds.
4. A peptide bond is formed between the 1st amino acid (methionine) and the second amino acid.
This is catalyzed by an enzyme called (Peptidyl transferase).
5. The first tRNA detaches leaving the 1st amino acid bonded to the second one.
6. The ribosome moves one more codon reading the 3rd codon. So, a 3rd tRNA comes bringing
the 3rd amino acid.
7. A peptide bond is formed between the 2nd and 3rd amino
acids and the 2nd tRNA detaches.
8. This process continues until a stop codon is reached.
9. Now the primary structure of the protein is synthesized.
› Summary: translation is the process in which a
ribosome reads mRNA codons and brings tRNA with
complementary anticodons. Hydrogen bonds are
formed between codons and anticodons while peptide
bonds are formed between amino acids. This occurs in the cytoplasm (ribosome).
N.B A ribosome consists of ribosomal RNA and proteins.

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Comparison between mRNA vs. tRNA
Points of Comparison mRNA tRNA

› Straight molecule. › Folded molecule.

› No hydrogen bonds. › Has hydrogen bonds.
Structure › Has codons. › Has anticodons.
› No amino acids › Has amino acids
binding site. binding site.
Location Nucleus & Cytoplasm Cytoplasm only

It’s formed from the templates It’s a folded molecule with

strand of DNA during anticodons on one side and an
transcription in the nucleus. Its amino acid on the other side.
codons are complementary to During translation tRNA
Function
genetic codes of DNA. It anticodons form H-bonds with
moves to the ribosome where mRNA codons. This ensures
it’s translated into a proper positioning of amino
polypeptide chain. acids in the polypeptide chain.

N.B The start codon is responsible for starting the amino acid sequencing process and bringing the
first amino acid. The stop codon is responsible for ending amino acid sequencing process and
releasing the polypeptide chain. It doesn’t bring an amino acid.

Mutations
Definition
Random change in the DNA nitrogenous base sequence which might alter protein structure. It
mostly occurs during DNA replication. It may be through insertion, deletion or substitution of a
nitrogenous base.
Causes
› Chemical mutagens: Ex. Tar, Tobacco smokers or Asbestos.
› Radiation mutagens: Ex. X-ray, Ionizing radiations.
Types
1. Neutral mutations:
The function of the protein is unchanged, this may be due to:
• One codon is altered. However, the new codon still codes for the same amino acid.
• A certain codon is changed. So, different amino acid exists in the 1ry structure, but it
doesn’t significantly affect the folding of the polypeptide chain.
2. Frame shift mutations:
All the codons in the sequence are altered, this may be caused by addition of a nucleotide (insertion
mutation) or removal of a nucleotide (deletion mutation).
3. Non-sense mutations:
The altered codon becomes a stop codon. So, the protein is half formed (mostly not functioning).
© Dr. Mohab Megahed 54
Genetic Diseases
› Definition:
A disease caused by a faulty allele on an autosome.
› Types:

Recessive inherited Dominant inherited

Definition The faulty allele is a recessive The faulty allele is a dominant allele
allele (e.g. Cystic fibrosis) (e.g. Achondroplasia)
Alleles F: normal A: Below average height
f: diseased a: Average height
Genotype FF: normal AA: diseased
options Ff: normal (carrier) Aa: diseased
ff: diseased aa: normal
N.B Carrier: Normal phenotype and heterozygous genotype. Carriers only exist in recessive
inherited genetic disorders.
N.B If two normal parents gave rise to a diseased child, the following conclusions are made:
1) The disease is recessive inherited.
2) The parents are heterozygous (carriers).
3) The diseased child is homozygous recessive as this child must have inherited two recessive
alleles, one from each parent.

© Dr. Mohab Megahed 55

Cystic Fibrosis
› Definition:
A recessive inherited genetic disorder caused by mutation in the CFTR gene (Cystic Fibrosis
Transmembrane Regulator protein) which is a large gene located on chromosome 7, leading to
abnormal CFTR protein which ends by sticky mucus.

› Mechanism:
Normally › CFTR protein allows exit of
Cl- outside epithelial cells.
› Na+ is drawn into mucus from
the intercellular space to
balance the charge. It passes
between epithelial cells.
› NaCl makes the mucus
hypertonic.
› Water enters mucus from the
cytoplasm by osmosis and it
becomes diluted (watery).
In Cystic Fibrosis › CFTR is blocked or absent so
Cl- stays inside the epithelial
cells.
› Na+ doesn’t move into mucus
as there is no change in
charges to balance.
› Mucus is hypotonic.
› Water leaves mucus to
cytoplasm by osmosis and it
becomes sticky.

› The sticky mucus in CF affects:

1. Lungs.
2. Digestive system.
3. Reproductive system.

© Dr. Mohab Megahed 56

 › Symptoms:
• Lungs:
Mucus produced is too sticky and blocks small
airways leading to alveoli.
1. Less air entry into alveoli leads
to a non-steep concentration
gradient between alveoli and
blood, so less gas exchange by
diffusion. This leads to less
oxygen in blood, so less aerobic
respiration, leading to less
energy being available which
reduces growth and leads to
easy fatigue.
2. Sticky mucus can’t be removed
by cilia so it accumulates.
Mucus provides optimum
conditions for bacterial growth,
so chest infections are very common.
• Reproductive system:
§ Mucus blocks Vas deferens in males and Fallopian tubes in females so
fertilization can’t occur (causing sterility).
• Digestive system:
§ Mucus blocks the bile duct and the pancreatic duct.
§ Enzymes do not reach the small intestine, this leads to improper digestion,
malnutrition and may result in weight loss.
§ Due to auto-digestion of the pancreas (when its enzymes return back to it),
Insulin is not formed leading to diabetes mellitus.

© Dr. Mohab Megahed 57

 › Lines of Treatment:
No definite treatment, symptomatic treatment might include:
1. Physiotherapy: to remove mucus from the lungs as much as possible to allow for entry of
air, using Positive Expiratory Pressure (PEP) and rhythmical tapping of the chest.
2. Drug therapy: such as mucolytics to dissolve mucus, antibiotics to treat bacterial infections
& vaccination to prevent new infections and insulin to treat (DM).
3. Challenging infertility: by IVF (In-Vitro Fertilization).
4. Organ transplantation: if the lungs are severely impaired.
5. Nutrition through IVF fluids.

Genetic Screening
Definition
Carrying out genetic analysis on a large number of people to identify carriers.
› In this process, samples are removed containing diploid somatic cells. (For example:
from the lining of the cheek)
› Gametes can’t be used in screening as they are haploid with half the DNA only. This
carries very high chances of having a false negative test result.
› Cystic fibrosis might arise from a wide range of different mutations in the CFTR gene, so
we should screen for all these possible mutations to avoid having a false negative test
result.
› When we identify carriers, we screen the rest of the family members in order to know if
they’re also carriers or not. This provides them with a real opportunity of making
informed choices.
Benefits
1. Reduce money spent by the health authorities, as usually the cost of treating an ill person is
higher than the cost of screening a large number of people.
2. Identifies carriers who can make their decision consequently, they have a variety of decisions:
a. To have children hoping to be lucky as only 1 in 4 are diseased.
b. Not to have children at all.
c. To get pregnant then undergo prenatal testing.
N.B. A negative screening test result makes the chances of having a diseased child very low but not
zero, because mutation might occur during the formation of gametes, a mutation might occur after
fertilization or the test itself might be false negative!

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Genetic testing:
This could be either pre-implantation genetic diagnosis or prenatal testing.
Pre-Implantation Genetic Diagnosis (PIGD):
› Gametes are fertilized in vitro by IVF and the resulting embryos are then tested. Only
embryos known not to have the disease are implanted into the uterus.
› Disadvantage: during IVF, the female is given high doses of hormones which might be
carcinogenic.
Prenatal testing
› Chorionic villus sampling:
A needle is inserted through the cervix to remove a couple of chorionic villi
as the placenta is formed of fetal cells. Fetal DNA is analyzed, looking for
the defective gene. This is done at week 8 and requires no culture
• Advantages: Earlier so the termination decision is less
traumatic
• Disadvantages: Has high risk of miscarriage.
› Amniocentesis:
A long needle is inserted through the mother’s abdomen into the amniotic
fluid of the developing embryo, as amniotic fluid is produced by the embryo
so it will have fetal cells. Fetal DNA is analyzed looking for the defective gene. This is done at week
16 and requires culture for 3 weeks.
• Advantages: Has less risk of miscarriage.
• Disadvantages: It is relatively late and the decision of termination may be traumatic
to the parents.
Ethical & social implications of Genetic testing:
Ethical:
• Embryo (or fetus) is a potential life and and discarding the embryo/deciding abortion might
be a murder.
Social:
• It might give rise to marital conflicts about who has the right to decide if the test should be
done and who has the right to determine the next step (termination or continuation).
• Parental & child DNA are both analyzed. Disclosure of genetic information affects future
employment & insurance profile.
• The test maybe false negative leading to continuation or false positive leading to termination.

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Genetic Counseling
› Trained persons known as genetic counselors offer help to those carrying the disease or having
strong positive family history. This help includes:
1. Awareness about the disease and how to deal with it.
2. Discussing all options for the decisions to be made according to the ethical, social or religious
views.

Sex linked disorders

› Definition:
Genetic disorders caused by a faulty allele on a sex chromosome (X chromosome). They can be
passed to the offspring.
› Types of sex-linked disorders:
1. Recessive inherited disorders
2. Dominant inherited disorders
Recessive inherited disorders
› Examples: Red green colour blindness & Haemophilia.
› Allele options:
XR: normal
Xr: diseased
› Genotype options:
XRXR: normal
XRXr: normal (carrier)
XrXr: diseased
XRY: normal
XrY: diseased
› Question:
Red green colour blindness is a sex-linked genetic disorder. Draw a genetic diagram
showing the offspring of a normal male and a carrier female. Allele options: XR:
normal, Xr: diseased.

© Dr. Mohab Megahed 60

N.B Explain why sex-linked recessive disorders are more common in males.
The male is XY so he has only 1 allele. If this allele is recessive, he will have the disease. This
is unlike a female who is XX, so to be diseased she must inherit 2 recessive alleles, one from
each parent.
Dominant inherited sex-linked disorders
› Example: Night blindness
› Allele options:
XN: diseased
Xn: normal
› Genotype options:
XNXN: diseased
XNXn: diseased
XnXn: normal
XNY: diseased
XnY: normal

© Dr. Mohab Megahed 61

© Dr. Mohab Megahed 62
Introduction to Investigation Questions
1. Variables of an investigation
› Independent variable: The variable changed by the experimenter (the one you decide about)
› Dependent variable: The variable measured by the experimenter (the one you measure)
› Controlled variables: The variables that must be kept constant during the investigation as
they might affect the results.
2. Aspects of an investigation
› Accuracy:
• Accuracy can be defined as the difference between actual values and measured values.
The higher the difference the lower the accuracy and vice versa.
• Accuracy is increased by changing the measuring method and using a more sensitive
measuring apparatus.
› Validity:
• This means how correct is your experimental procedure.
• Validity is increased by keeping all other factors constant to have a fair test (controlled
variables).
› Reliability:
• This means how similar your results are after several replications.
• Error bars/ Range bars show spread of data around the mean. So, they give an
indication on the variability of data.
• The larger the error bars, the wider the data variability
and the lower the data reliability (& vice versa).
• If error bars are overlapping, this reduces data
reliability.
• Standard deviation (SD) is similar to error bars but
it takes the sample size into consideration. It is equal
sized on both sides of the mean.
• Reliability is increased by controlling all variables
and measuring the dependent variable accurately.
• Repetition only measures reliability but doesn’t
increase it (if repetition by other scientists gave
similar results this enhances reliability)

3. Data tabulation
› Independent Variable: comes in the first column in vertically oriented graphs OR upper
row in horizontally oriented graphs.
› Dependent Variable: comes in the second column in vertically oriented graphs OR lower
row in horizontally oriented graphs.
› Include SI units in the headings of your columns / rows.

© Dr. Mohab Megahed 63

Remember:
!"# %& '()*+,-.
› You may be asked to calculate the mean = , then you might include the
/0(+' ,"#1('
mean in a third column in your table.

4. Data presentation in Graphs

› Independent variable on X-axis.
› Dependent variable on Y-axis.
› Use more than 50% of both axes.
› Plot all points accurately. Use circled dots or crosses.
› Join points with neat straight lines, don’t extrapolate.
› Don’t forget the SI units in your axes labels.
Remember: Your comment on a given graph should include description of the trend, pattern & data
manipulation (subtraction, division or percentage change). Don’t make theoretical assumptions
except if you were asked to explain the changes shown by the graph.
Don’t comment on minor changes like a small drop or increase between two points except if it has
a clear biological significance

N.B. Some commonly used technical terms:

• Precise results: They are results taken using a sensitive instrument that measures to smaller
increments. (readings with more decimal places)
• Qualitative: a qualitative test tells you what is present. It has the disadvantage of being
subjective.
• Quantitative: a quantitative test tells you how much is present. It has the advantage of being
objective.
• Random errors: unpredictable non consistent errors that occur while taking measurements.
They can affect each individual measurement in a random way and they affect the pattern of
change by producing anomalous results (outliers)
• Systematic errors: quantified consistent errors affecting all measurements. They don’t affect
the pattern of change. They most commonly arise from poor calibration of the measuring
equipment. For example, if a stop watch is faulty and runs 10% slower than normal, then all
timings will be underestimated by 10%.
• Hypothesis: a conclusion based on an observation.

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Unit 1 Core Practical
N.B Types of tests:
1) Quantitative test: tells how much of a certain substance is present.
2) Qualitative test: tells if the substance is present or not with no indication on quantity.
3) Semi quantitative test: gives an estimate of the present quantity of a substance.

1. Semiquantitative food tests

Testing for reducing sugars
› Add the food sample to water and mix properly.
› Add a known volume of Benedict’s reagent.
› Heat in a water bath at 95oC for a few minutes.
› If colour changes from pale blue into brick red, then much glucose is present (Positive
test).
› Colour changes:
1) Pale blue = no glucose
2) Green = traces of glucose 0.5%
3) Yellow = low level of glucose 1%
4) Orange = moderate level of glucose 1.5%
5) Brick red = high level of glucose >or =2.0%

Testing for proteins

› Add the food sample to water and mix carefully.
› Add a known volume of Biuret’s reagent.
› If colour changes from blue into purple, proteins are present (Positive
test)
Testing for starch
› Add iodine to the food sample.
› If colour changes from yellow-brown into blue-black then starch is
present.

How are these tests semi quantitative?

› To have a semi quantitative test a colorimeter is used to
measure the absorbance of colour or transmission of
light.
› By detecting the colour intensity we can estimate the
concentration of substance X by using a calibration
curve which shows the intensity of colour (on the Y-
axis) plotted against the concentration of substance X
(on the X-axis).
› The deeper the colour, the higher the concentration of
substance X.

© Dr. Mohab Megahed 65

 2. Investigating Vitamin C content of different juices
› Add 2 cm3 of 0.1% DCPIP to a test tube.
› Prepare juices from both fruit species using the same
extraction method.
› Use a pipette to add equal sized drops of the tested juice
using a pipette to the test tube containing the blue
DCPIP solution.
› Shake well after each drop.
› Records the number of drops needed to change DCPIP from blue to colourless.
› Repeat the process and calculate the average.
› To compare vitamin C concentration of different juices, use number of drops as a
reference.
› The higher the number of drops needed to decolorize DCPIP, the lower is vitamin C
concentration and vice versa.
› To increase accuracy, use a calibrated pipette to measure the exact volume of juice
needed to decolourize DCPIP.
› To know the exact vitamin C concentration of the tested juice you can use a calibration
curve OR repeat the process with a standard vitamin C juice (solution of known
concentration) & record the results then use the following equation:

Conc. B = (Vol. A * conc. A)/ vol.B

Vol. A = volume of Vitamin C solution in ml
Conc. A = Concentration of vitamin C solution in mg/ml
Vol. B = Volume of fruit juice in ml
Conc. B = concentration of vitamin C in fruit juice in mg/ml
Independent variable: fruit juice
Dependent variable: volume of juice required to decolorize 1 cm3 of DCPIP.
Controlled variables:
› Temperature of the surroundings.
› Volume and concentration of DCPIP solution.
› Extent of shaking the tube.
› Same end point colour

© Dr. Mohab Megahed 66

 3. Effect of temperature on cell membranes
› Cut equal sized pieces of fresh beetroot using a cork borer.
› Rinse all discs under fresh water for 5 minutes to remove any pigment
produced from cutting.
› Add six cubes of beetroots to a test tube.
› Add 5 cm3 of distilled water to the test tube.
› Prepare a water bath set at 10oC using a large beaker, tripod, gauze and
Bunsen burner (wear goggles) and place the test tube in it.
› Leave beetroots for an hour.
› After the hour, shake the tube and hold it to light to observe the
color of the solution.
› Repeat the exact same procedure for other test tubes with
temperatures 20, 30, 40, 50 & 60oC
› Compare colors of solution in different test tubes.
› To improve accuracy, use a clean cuvette & a colorimeter which
could either measure transmission of light or absorbance of
color.
› To ensure validity, control all variables such as…
Independent variable: Temperature of water.
Dependent variable: Absorbance of color from the resulting solution.
Controlled variables:
› Volume of distilled water in the test tubes.
› Number of beetroot cubes in the test tubes.
› Time left in water.
› Size of beet root cubes.
› Storage age and storage conditions of beetroots.
Expected outcome:
As the temperature increases, the intensity of red color increases. Beetroots have Betalain pigment
stored in their vacuoles, High temperatures causes coagulation of membrane proteins & melting of
the phospholipid bilayer leading to loss of selective permeability and escape of the Betalain pigment
from the vacuole into cytoplasm then outside the cells into water.
N.B. Alcohol also causes loss of membrane permeability as it dissolves the phospholipid
bilayer. To investigate the effect of alcohol on membrane permeability, the same investigation
is repeated but with using a range of alcohol concentrations and fixing the temperature.

© Dr. Mohab Megahed 67

 4. Effect of Changing Substrate Concentration on the Rate of Reaction

› Use a large syringe to measure 20 cm3 of pureed potato into a conical flask
› Connect this conical flask using a delivery tube to a half-full water bowl with an inverted
measuring cylinder.
› Measure 2 cm3 of Hydrogen peroxide using a syringe and add them to the pureed potato.
› After, 30 seconds note the volume of oxygen in the measuring cylinder.
› Divide the volume of oxygen given out by 30 to get the initial rate of reaction in terms of
cm3/s
› Repeat the whole process using different concentration of H2O2 such as 30, 40 & 50 cm3
› Record the results in a table.
› Plot a graph showing the effect of changing H2O2 concentration on the rate of reaction.
› To ensure validity, control temperature using a thermostatic water bath and control pH by
adding buffer solution.
› To ensure reliability, repeat several times for each concentration of catalase and calculate the
average rate of reaction.
N.B Why use catalase?
1) Abundant in nature as it’s found in most living organisms.
2) It’s an enzyme with very high specific activity.
3) The product is oxygen gas which is easy to measure.
Independent variable: substrate concentration
Dependent variable: Initial rate of reaction at each concentration.
Controlled variables:
› Temperature
› pH
› Volume & concentration of the enzyme.
› Volume of the substrate

N.B. To investigate the effect of enzyme concentration on the rate of reaction, repeat the same
investigation but with varying the volume of pureed potatoes used and fixing H2O2
concentration.

Good Luck J

© Dr. Mohab Megahed 68