Structure and function of Haemoglobin 3.57.51 PM

Structure and function of Haemoglobin 3.57.51 PM -...

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Unformatted text preview: Structure and function of Haemoglobin Dr. Tariq M Roshan Department of Hematology PPSP Introduction The main function of red blood cell Transfer of O2 from lungs to tissue Transfer of CO2 from tissue to lungs To accomplish this function red cells has haemoglobin (Hb) Each red cell has 640 million molecules of Hb Introduction Introduction Haemoglobin (Hb), protein constituting 1/3 of the red blood cells Synthesis begins in proerythroblast 65% at erythroblast stage 35% at reticulocyte stage Two parts Haem Globin Synthesis of Haemoglobin (Hb) Synthesis of Haemoglobin (Hb) Haem & globin produced at two different sites in the cells Haem in mitochondria Globin in polyribosomes Well synchronized Synthesis of Haemoglobin Synthesis of Haemoglobin Synthesis of Haem Synthesis of Haem Protoporphyrin ring with an iron atom in centre The main site is mitochondria as it contains ALAS Mature red cell does not contain mitochondria Structure of Haem Structure of Haem Synthesis of globin Synthesis of globin Synthesis of globin Synthesis of globin Various types of globin combines with haem to from different haemoglobin Eight functional globin chains, arranged in two clusters the β­ cluster (β, γ , δ and ε globin genes) on the short arm of chromosome 11 α­ cluster (α and ζ globin genes) on the short arm of chromosome 16 Globin gene clusters Globin gene clusters Synthesis of globin Globin synthesis, starts at 3rd week of Globin synthesis, starts at 3 gestation Embryonic Haemoglobin Gower I ( ζ2ε2) Haemoglobin Portland ( ζ2γ 2) Haemoglobin Gower II (α2ε2 ) Fetal : HbF (α2γ 2), HbA (α2β2) Adult : HbA, HbA2 ( α2δ2), HbF. Globin chain switch Globin chain switch Alpha & beta chains Alpha & beta chains Adult haemoblobin Hb A Hb A Hb A2 Hb F structure 2β2 22 2γ 2 Normal % 96­98 % 1.5­3.2 % 0.5­0.8 % Functions of Haemoglobin Functions of Haemoglobin Oxygen delivery to the tissues Reaction of Hb & oxygen Oxygenation not oxidation One Hb can bind to four O2 molecules Less than .01 sec required for oxygenation β chain move closer when oxygenated chain move closer when oxygenated When oxygenated 2,3­DPG is pushed out β chains are pulled apart when O2 is unloaded, chains are pulled apart when O permitting entry of 2,3­DPG resulting in lower affinity of O2 Oxy & deoxyhaemoglobin Oxy & deoxyhaemoglobin Oxygen­haemoglobin dissociation Oxygen­haemoglobin dissociation curve O2 carrying capacity of Hb at different Po2 Sigmoid shape Binding of one molecule facilitate the second molecule binding P 50 (partial pressure of O2 at which Hb is half saturated with O2) 26.6mmHg Hb­oxygen dissociation curve Hb­oxygen dissociation curve Hb­oxygen dissociation curve The normal position of curve depends on Concentration of 2,3­DPG H+ ion concentration (pH) CO2 in red blood cells Structure of Hb Hb­oxygen dissociation curve Right shift (easy oxygen delivery) High 2,3­DPG High H+ High CO2 HbS Left shift (give up oxygen less readily) Low 2,3­DPG HbF Summary Summary Normal structure including the proportion of globin chains are necessary for the normal function of haemoglobin Reduced haemoglobin in the red blood cells due to any abnormality of any of its constituents result into a clinical situation called anaemia Metabolic & other abnormalities result into abnormal oxygen supply to the tissue ...
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