💗HAEMOGLOBIN SYNTHESIS AND FUNCTION💗
💘Hello my dear viewers🙋....first of all, do you know what is heamoglobin ???Aikkk…. Don’t know ??? If you don’t know, do read our post okay😇
Nahhhhh.... Have you read the synthesis of haemoglobin and the function of erythropoiesis??? If no,
now let me tell you about synthesis and function of erythropoiesis💗.
Are you ready ??? Okay okay. Don’t worry😉. I will just
explain briefly about the synthesis and funcion of haemoglobin. If you want more, do
follow us okay💛😊.
WHAT IS HAEM??
v Haem is actually an iron containing compound of porphyrin class which forms the non – protein of haemoglobin and some other molecule.
v Haem synthesis occur largely in the mitochondria.
HOW ABOUT GLOBIN??
v Superfamily of haem containing globular protein and involve in binding, transporting oxygen.
v Globin synthesis occurs in the polyribosome.
WHAT IS HAEMOGLOBIN?
v Did you know that?? Haemoglobin is a protein molecule in the red blood cell that carries oxygen from lungs to the tissues and return carbon dioxide from tissue to lungs to be exhaled out. Molecular weight of the haemoglobin are about 68000 and comprise one third of a red cella. Haemoglobin is formed from the combination of haem and globin.65% of the haemoglobin will be synthesised in the erythroblast and the remaining 35% at the reticulocyte stage. A normal person would have haemoglobin HB-A that consist of four polypeptide chains a2B2 each with its own haem group.
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HAEMOGLOBIN SYNTHESIS
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| Haemoglobin synthesis |
v Haem synthesis begins with the condensation of glycine and succinyl-CoA to form δ-aminolevulinic acid (ALA). ALA then leaves the mitochondria and form porphobilinogen through a series of reaction forms coproporphyrinogen. This molecule then returns to the mitochondria and produce protoporphyrin.Proto-porphyrin is then combined with iron to form haem. Haem then exits the mitochondria and combines with the globin molecule which is synthesized in the ribosome.
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FUNCTION OF HAEMOGLOBIN
My dear viewers💛,the hemoglobin💗 molecules with the help of external chemical factors take up oxygen molecules in the lungs and then send them to the various tissues of our body. The biggest regulator of oxygen affinity in the hemoglobin💗 is the oxygen itself. If in lungs, the oxygen levels are high the hemoglobin shows greater affinity towards the oxygen molecules and as it bounds to more oxygen, this property of affinity increases and vice versa. When the oxyhemoglobin binds to the maximum capacity, it becomes saturated but its affinity towards oxygen increases⇑ whereas when this binding loose oxygen molecule the affinity decreases⇓. This regulation activity is called as cooperativity and is an important function as it allows maximum amount of hemoglobin💕 to be carried to the tissues and also allows deoxyhemoglobin which is releasing the oxygen tissue. And yeah guys🙋,the external chemical factors which help in regulation of oxyhemoglobin affinity includes pH, DPG (2, 3-diphosphoglycerate) and carbon dioxide.
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