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Haemoglobin

Heemoglobin

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Kaushal wagh
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17 views10 pages

Haemoglobin

Heemoglobin

Uploaded by

Kaushal wagh
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Hemoglobin

• Hemoglobin is the iron containing coloring


matter of red blood cell.
Structure of Hemoglobin-
o It consists of a protein combined with an
iron-containing pigment
o The protein part is globin
o Iron containing pigment is heme
▪ Iron-It is present in ferrous (Fe2+) form. It is
in unstable form.
▪ Porphyrin-
o The pigment part is called Porphyrin.
o It is formed by 4 pyrole rings.
o The iron is attached to N-of each pyrole
ring & N-of globin molecule.
▪ Globin-
o contains 4 polypeptide chains.
o 2 alpha & 2 beta chains.
Normal Values-
o At Birth : 22-24 gm%
o After 3rd Month : 18-20 gm%
o After 1 year : 15-17 gm%
o Adult male : 13-15 gm%
o Adult female : 12-14.5 gm%

Derivatives of Hemoglobin-
Hemoglobin readily combines with gas & other
substances to form some products, which are called
derivatives of Hemoglobin.
1. Oxy-hemoglobin
o Combination of Hb with Oxygen
o Unstable compound, combination is
reversible
2. Carbamino-hemoglobin-
o Combination of Hb with CO2
o Affinity of Hb for CO2 is 20 times more
than oxygen.
3. Carboxy-hemoglobin-
o Combination of Hb with carbon monoxide
o Affinity of Hb for Carbon monoxide is 200
times more than oxygen.
4. Sulf-hemoglobin-
o Combination of Hb with H2S
Types of Hemoglobin-

1. Adult hemoglobin -HbA= 2 alpha & 2 beta


chains
2. Fetal hemoglobin -HbF= 2 alpha & 2 gamma
chains
Synthesis of Hemoglobin-

SYNTHESIS OF HEME-
Heme is synthesized from succinyl-CoA and the
glycine.
• Heme portion of hemoglobin is synthesized in
mitochondria
• 2 molecules of succinyl CoA combine with 2
molecules of glycine to form Pyrole compound.
• 4 pyrole compounds combine to form
Protoporphyrin.
• Protoporphyrin combines with iron to form
heme.
FORMATION OF GLOBIN-
o Polypeptide chains of globin are produced
in the ribosomes.
o There are four types of polypeptide chains
namely, alpha, beta, gamma and delta
chains.
o Each of these chains differs from others by
the amino acid sequence.
o Adult hemoglobin contains two alpha
chains and two beta chains. Fetal
hemoglobin contains two alpha chains and
two gamma chains.
CONFIGURATION-
• Each heme molecule combines with one globin
molecule to form Hemoglobin.
Destruction of Hemoglobin-
o Iron (Fe)- stored in the body as ferritin &
hemosiderin, which is utilized for synthesis
of new hemoglobin.
o Globin- stored in the body as amino acids &
utilized for synthesis of new hemoglobin.
o Porphyrin- converted into biliverdin &
further into bilirubin which is excreted out
from the body.
Functions-
1. Transport of respiratory gases-
Oxygen from lungs to tissues:
o When oxygen binds with hemoglobin, a
physical process called oxygenation occurs,
resulting in the formation of
oxyhemoglobin.
o The iron remains in ferrous state in this
compound.
o Oxyhemoglobin is an unstable compound
and the combination is reversible, i.e. when
more oxygen is available, it combines with
hemoglobin and whenever oxygen is
required, hemoglobin can release oxygen
readily.
o When oxygen is released from
oxyhemoglobin, it is called reduced
hemoglobin or ferrohemoglobin.
2. CO2 from tissues to lungs
o When carbon dioxide binds with
hemoglobin, carbamino-hemoglobin is
formed.
o It is also an unstable compound and the
combination is reversible, i.e. the carbon
dioxide can be released from this
compound. The affinity of hemoglobin for
carbon dioxide is 20 times more than that
for oxygen
3. Buffer action- plays an important role in acid
base balance
ABNORMAL HEMOGLOBIN-
1. Hemoglobin S: It is found in sickle cell anemia.
In this, the α-chains are normal and β-chains are
abnormal.
2. Hemoglobin C: The β-chains are abnormal. It is
found in people with hemoglobin C disease,
which is characterized by mild hemolytic
anemia and splenomegaly.
3. Hemoglobin E: Here also the β-chains are
abnormal. It is present in people with
hemoglobin E disease which is also
characterized by mild hemolytic anemia and
splenomegaly.
4. Hemoglobin in Thalassemia-
o In thalassemia, different types of abnormal
hemoglobins are present.
o The polypeptide chains are decreased,
absent or abnormal. In α-thalassemia, the
α-chains are decreased, absent or abnormal
and
In β-thalassemia, the β-chains are
decreased, absent or abnormal.

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