Haemoglobin is composed of heme and globin proteins. It transports oxygen from the lungs to tissues via its reversible binding to oxygen. Haemoglobin is synthesized through coordinated production of heme in mitochondria and globin chains in the cytosol. The most common adult haemoglobin variant is HbA, while fetal haemoglobin is HbF. Haemoglobin levels and variants are important for oxygen delivery and conditions like diabetes.
Haemoglobin is composed of heme and globin proteins. It transports oxygen from the lungs to tissues via its reversible binding to oxygen. Haemoglobin is synthesized through coordinated production of heme in mitochondria and globin chains in the cytosol. The most common adult haemoglobin variant is HbA, while fetal haemoglobin is HbF. Haemoglobin levels and variants are important for oxygen delivery and conditions like diabetes.
Haemoglobin is composed of heme and globin proteins. It transports oxygen from the lungs to tissues via its reversible binding to oxygen. Haemoglobin is synthesized through coordinated production of heme in mitochondria and globin chains in the cytosol. The most common adult haemoglobin variant is HbA, while fetal haemoglobin is HbF. Haemoglobin levels and variants are important for oxygen delivery and conditions like diabetes.
Haemoglobin is composed of heme and globin proteins. It transports oxygen from the lungs to tissues via its reversible binding to oxygen. Haemoglobin is synthesized through coordinated production of heme in mitochondria and globin chains in the cytosol. The most common adult haemoglobin variant is HbA, while fetal haemoglobin is HbF. Haemoglobin levels and variants are important for oxygen delivery and conditions like diabetes.
Introduction • Haemoglobin is a red globular protein composed of heme (consisting of iron and protoporphyrin) and globin.
• Globin portion of the molecule consists of four (or two pairs) of polypeptide chains.
• Hb= 64,500 daltons contributing one third of weight of RBC.
• There are different haemoglobin variants, but all share the same basic structure of four globin polypeptide chains, each with heme group.
• Functional haemoglobin is composed of two pairs of dissimilar globins.
Normal values of Hb Haemoglobin Synthesis • Although haem & globin synthesis occur separately within developing red cell precursors, their rate of synthesis are carefully coordinated to ensure optimal efficiency of haemoglobin assembly.
• 65% of haem is synthesized in the erythroblasts.
• 35% of it at reticulocyte stage.
• Heme part occurs in the mitochondria and in the cytoplasm of RBC precursors. Haem synthesis • This reaction is energy dependent and so occurs in the mitochondria.
• It's catalyzed by the enzyme ALA synthase.
• This step is a rate-limiting step for the whole process of heme synthesis. • It is stimulated by the presence of globin chains and inhibited by the presence of free heme groups. Haem Globin Synthesis • Humans normally carry 8 functional globin genes, arranged in two gene clusters. • The alfa-like cluster on the short arm of chromosome 16. • The ß-like cluster on the short arm of chromosome 11. • These genes code for 6 different types of globin chains: a, ß, y, delta, epsilon, zeta globin. Globin Chains • Globin chains are synthesized in the cytosol of erythrocytes.
• Consists of varied sequences of AA: polypeptide chains.
• These are Alpha (a), Beta (B), Gamma (v), Delta (5), Epsilon (E) and Zeta (3).
• The sequence and the number of AA in the chain are different.
HAEMOGLOBIN STRUCTURE • Haemoglobin is a tetramer composed of 4 polypeptide chains and 4 heme groups.
• Alfa chain consists of 141 amino acids while ß chain has 146 amino acids.
• Each polypeptide chain is arranged in a helical conformation
• Each RBC has 640 million molecule of Hb.
Haemoglobin variants Adult Hb(Hb A): • Hb A1(2a & 2ß subunits) is the major form of Hb 96-98% in adults & in children over 7 months of age.
• Hb A2 (2a & 2delta subunits) is the minor form of Hb in adults.
• It forms only 2.2-3.5% of total Hb A.
• Poor form of Hb for oxygen carriage.
Fetal Hb (Hb F) • 2 аlfa & 2 gama subunits
• At birth, 50-95% of a baby's haemoglobin is HbF, but these levels decline
after 6 months as more HbA is produced.
• In a healthy adult, <1% of haemoglobin is HbF.
• The oxygen affinity of HbF is substantially greater than HbA to facilitate the transfer of oxygen. HbA1c: glycosylated haemoglobin
• Subtype of HbA1 • Attachment of glucose to valine (N terminal amino acid) of the beta chain of hemoglobin. • Indicator of how well the blood glucose level has been controlled over a long period of time( 2-3 months). • Its high value is directly related to complications from diabetes. Hb-COMPOUNDS AND DERIVATIVES
• 1. Oxyhemoglobin: • In oxy-Hb, Fe is in the ferrous form. • The binding of O2 to fe is loose (noncovalent) and hence it is easily reversible.
• 2. Methemoglobin: • In this type of Hb, Fe is in the ferric state. • Produced in small amount converted to oxyhemoglobin by methemoglobin reductase. • 3. Carboxyhemoglobin: • Due to the high affinity of CO for Нb, Нb binds with very little O2 in presence of CO. • Thus, tissue hypoxia results, which is a type of anemic hypoxia as the hemoglobin is rendered ineffective by CO. • 4. Carbaminohemoglobin: • CO2 combines with an NH2-group of an amino acid in the polypeptide chain of Hb to form carbamino-Hb
• 5. Acid and alkali hematin:
• These compounds are formed when Hb reacts with acids or alkalis. • 6. Hemin crystals: • Rhombic form of the crystals are formed when Hb in blood is boiled with NaCl and glacial acetic acid. • This has obvious medicolegal importance.
• 7. Bilirubin and biliverdin
Functions of Hemoglobin Functions of Hemoglobin • Transport of oxygen from the lungs to the tissues.
• Carriage of carbon dioxide from tissues to the
lungs as carbaminohaemoglobin.
• Buffering of hydrogen ions formed in the
erythrocyte from the conversion of carbon dioxide into bicarbonate.
