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Haemoglobin Synthesis

Hemoglobin (Hb) is a crucial protein in red blood cells responsible for transporting oxygen and carbon dioxide, comprising 95% of the dry weight of RBCs. Normal Hb levels vary by age and sex, with adult males averaging 15g/dl and females 14g/dl. The synthesis of Hb begins in the proerythroblastic stage, with heme produced in mitochondria and globin synthesized in ribosomes, ultimately forming a complete hemoglobin molecule with four polypeptide chains and four heme groups.

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6 views3 pages

Haemoglobin Synthesis

Hemoglobin (Hb) is a crucial protein in red blood cells responsible for transporting oxygen and carbon dioxide, comprising 95% of the dry weight of RBCs. Normal Hb levels vary by age and sex, with adult males averaging 15g/dl and females 14g/dl. The synthesis of Hb begins in the proerythroblastic stage, with heme produced in mitochondria and globin synthesized in ribosomes, ultimately forming a complete hemoglobin molecule with four polypeptide chains and four heme groups.

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arundurai6435
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© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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HEMOGLOBIN SYNTHESIS

 Hb is the iron containing coloring matter of red blood cells.

 It is a chromoprotein forming 95% of dry weight of RBC and 30% to 34% of wet weight.

 Its function is to carry the respiratory gases, oxygen and carbondioxide.

 It also acts as a buffer and its molecular weight is 68,000.

NORMAL HB COUNT:

 Average Hb content in blood is 14 to 16g/dl.

 The Hb values depends upon the age and sex of the individual.

 Age : at birth-25g/dl

 After 3rd month -20g/dl

 After 1 year- 17g/dl

 From puberty onwards-14-16g/dl.

 At the time of birth Hb count is high due to the increased number of RBCs.

 Sex:

 In adult males – 15g/dl

 In adult females-14g/dl

Hb FUNCTIONS:

 Transport of respiratory gases is the main function of Hb.

 Buffer action

 Oxygen from the lungs to tissues.

 Carbondioxide from the tissues to lungs.

TRANSPORT OF OXYGEN:

 When oxygen binds with Hb, a physical process called oxygenation occurs, resulting in the
formation of oxyhemoglobin.

 The iron remains in ferrous state in this compound.

 Oxyhemoglobin is a unstable compound and the process is a reversible.

 When oxygen is released from oxyhemoglobin. It is called reduced hemoglobin or


ferrohemoglobin.
TRANSPORT OF CO2:

 Carbhemoglobin is formed when co2 is combined with Hb.

 It is also unstable compound and the combination is reversible.

 The affinity of Hb for CO2 is 20 times more than that of oxygen.

BUFFER ACTION:

 Hb acts as a buffer and plays an important role in the maintenance of acid-base balance.

STRUCTURE OF Hb:

 Hb is a conjugated protein. It consists of a protein combined with an iron- containing


pigment.

 Protein part is ‘globin’ and the iron containing pigment is ‘heme’.

 Heme also forms the structure of myoglobin and neuroglobin.

 Iron – it is present in ferrous form (Fe2+). It is unstable or loose form. In some abnormal
condition, it is in ferric state (Fe3+) which is stable form.

 Porphyrin - The pigment part of the heme is called porphyrin. It is formed by the pyrrole
ring. These pyrrole rings are attached to one another by methane (CH4) bridges.

 Globin - It contains four polypeptide chains.

Hb SYNTHESIS:

 Synthesis of hemoglobin actually starts in proerythroblastic stage.

 However, hemoglobin appears in the intermediate normoblastic stage.


 Production of Hb continues until the stage of reticulocyte.

 Heme portion of the hemoglobin is synthesized in mitochondria and the globin part is
synthesized in ribosomes.

 Heme is synthesized from succinyl-coA and the glycine.

 It occurs in miochondrion. Two molecules of succinyl coA combines with two molecules of
glycine and condense to form 5- aminolevulic acid (ALA) by ALA synthase.

 ALA is transported to the cytoplasm. Two molecules of ALA combines to form


porphobilinogen in the presence of ALA dehydratase.

 Porphobilinogen is converted into uroporphobilinogen I by uroporphobilinogen synthase.

 Uroporphobilinogen I is converted into uroporphobilinogen III by porphobilinogen III


Cosynthase.

 From uroporphobilinogen III, a ring structure called coprophorphyrinogen III is formed by


uroporphobilinogen decarboxylase.

 Coprophorphyrinogen III is transported back to the mitochondrion, where it is oxidised to


form protoporphyrinogen IX by corprophyrinogen oxidase.

 Protoporphyrinogen IX is converted into protoporphyrin IX by protoporphyrinogen oxidase.

 Protoporphyrin IX combines with iron to form heme in the presence of ferrochelatase.

FORMATION OF GLOBIN:

 Polypeptide chains of globin are produced in the ribosomes.

 There are four types of polypeptide chains namely, alpha, beta,gamma, and delta chains.

 Each globin molecules is formed by the combination of 2 pairs of chains and each chain is
made of 141 to 146 amino acids.

 Adult Hb contains two alpha chains and two beta chains.

 Fetal hemoglobin contains two alpha chains and two gamma chains.

CONFIGURATION:

 Each polypeptide chains combines with one heme molecules.

 Thus after the complete configuration, each hemoglobin molecules contains 4 polypeptide
chains and 4 heme molecules.

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