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Structure Of Hemoglobin and Difference between Fetal and Adult Hemoglobin.

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Structure Of Hemoglobin and Difference between Fetal and Adult Hemoglobin.

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Structure Of Hemoglobin and Difference between Fetal and Adult Hemoglobin.

  1. 1. STRUCTURE OF HEMOGLOBIN & NORMAL RANGE DIFFERENCE BETWEEN FETAL AND ADULT HEMOGLOBIN Abdul Qadir Khan Roll No. 04 Batch 2016-17
  2. 2. Learning Objective  Introduction.  Structures Of Hemoglobin.  Types Of Hemoglobin.  Differences between Fetal and Adult Hemoglobin.  Bibliography.
  3. 3. Introduction Hemoglobin is the protein molecule in red blood cells that carries oxygen from the lungs to the body's tissues and returns carbon dioxide from the tissues back to the lungs.
  4. 4. Basic chemical steps in the formation of hemoglobin. • First, succinyl-CoA, formed in the krebs metabolic cycle, binds with glycine to form a pyrrole molecule. • In turn, four pyrroles combines to form protoporphyrin IX, which then combines with iron to form the heme molecule. • Finally, each heme molecule combines with a long polypeptide chain, a globin synthesized by ribosomes, forming a subunit of hemoglobin called hemoglobin chain.
  5. 5. • The primary function of hemoglobin in the body is to combine with oxygen in the lungs and then to release this oxygen readily in the peripheral tissue capillaries, where the gaseous tension of oxygen is much lower than in lungs. • Oxygen does not combine with the two positive bonds of the iron in the hemoglobin molecule.
  6. 6. • It binds loosely with one of the so-called coordination bonds of the iron atom. • This is an extremely loose bond, so the combination is easily reversible. • The oxygen does not become ionic oxygen but is carried as molecular oxygen to the tissues. • Because of the loose, readily reversible combination, it is released into the tissue fluids still in the form of molecular oxygen rather than ionic oxygen.
  7. 7. Structure Of Hemoglobin • The moleculer weight of hemoglobin is 64,458. • It is made up of two components: i) Heme and ii) globin. • Heme is a tetra-pyrrole structure with a central iron atom attached to four nitrogen atoms from four pyrrole rings.
  8. 8. • Globin is a protein containing two pairs of polypeptide chains. It binds to the same iron atom that binds the pyrrole rings. • One heme and one globin chain form a subunit. • Four such subunits form a hemoglobin structure.
  9. 9. • There are several slight variations in the different subunit hemoglobin chains, depending on the amino acid composition of the polypeptide portion. • The different types of chains are designated Alpha chains, Beta chains, Gamma chains, and Delta chains. • The most common form of hemoglobin in the adult human being, hemoglobin A. • The most important feature of the hemoglobin molecule is its ability to combine loosely and reversibly with oxygen.
  10. 10. Types Of Hemoglobin 1. Adult Hemoglobin (HbA) 2. Fetal Hemoglobin (HbF- α2γ2) 3. Hemoglobin-S (HbS) 4. Miscellaneous Hemoglobin
  11. 11. Difference between Fetal & Adult Hemoglobin • Hemoglobin A is composed of two alpha and two beta chains while Hemoglobin F is composed of two alpha and two gamma chains. • Fetal hemoglobin life span is less (about 80 days) as compared to that of HbA (120 days). • Fetal Hb has greater affinity for oxygen as compare to the Adult Hb mainly to facilitate more oxygen supply to the developing fetus.
  12. 12. • The fetal hemoglobin production is switched off after birth, after that a normal child start producing Adult hemoglobin. • Adult hemoglobin is present in major amount almost above 90% in normal human after birth, while fetal hemoglobin is decreased to 2% due to production of adult hemoglobin.
  13. 13. Bibliography • Guyton & Hall • A K Jain • D. Venkatesh • Google Images

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