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Haemoglobin

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Published in: Biology | Physiology
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Haemoglobin Composition, Function, Synthesis, and Effect on the BodySystem.

Meenali M / Delhi

7 years of teaching experience

Qualification: M.Sc (Amity university - 2017)

Teaches: Anatomy, Biology, Physiology, Zoology, All Subjects, Mathematics, Physics, Chemistry, Story Telling, Unix/Linux

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  1. HAEMOGLOBIN ß chain chain STRUCTURE ,FUNCTION SYNTHESIS MEENALI MISHRA 2+ Heme
  2. WHAT IS HAEMOGLOBIN? aRespiratory pigment found in red blood corpuscles. oConjugated protein oSynthesised inside immature erythrocytes. aGives red color to the cell. olron containing oxygen metalloprotein. oConsist of two compounds -haem -globin
  3. HAEMO€LOBIN STRUCTURE oVariety of Hb molecule produced in humans OAII tetramers consisting numerous combination OSeven distinct polypeptide chain OEncoded by a separate gene. oHbA1 contains 2 a and 2 subunits o a chains contain 141 aminoacids residue chains contains 146 aminoacids residue
  4. STRUCTURE OF HbA1 j!chain t a che;.l —llcmo eye oeh8in2 Hemoglobin molecule 1 Heme
  5. STRUCTURE OF HAEMo a o a o Haem group consist of an iron (Fe) held in a heterocycle ring known as a porphyrin . This ring consist of four pyrrole molecule cyclically linked by methane bridges. Protoporphyrin compound combines with metal iron forming metalloporphyrin. Metal iron is 0.34% Fe is in ferrous state.
  6. tetrapyrrol methane brid STRUCTURE OF cyclic METALLOPORPHYRIN CH2=HC CH2 CH H3C H3C 2004 Thomson - Brooks Cole CH3 CH2CH2COi H2CH2C02- pyrrole
  7. STRUCTURE OF GLOBIN oConsist of tetramers with two polypeptide chains aHelps haem to keep iron in ferrous state aCombine loosely and reversibly with Oxygen
  8. Hemoglobin Molecule iron o chain heme group # chain red blood cell chain p' chain helical shape of the polypeptide molecule
  9. STRUCTURE OF HAEMOGLOBIN 065% of Hb is synthesized in the erythroblasts, 0 35% at the reticulocyte stage. DHaem synthesis occurs largely in the mitochondria. DGlobin synthesis occurs in the polyribosomes
  10. SYNTHESIS OF HAEMO€LOBIN re •Haem synthesis starts with condensation of glycine succinyl coenzyme A o under the action of a rate limiting enzyme ö- aminolaevulinic acid synthase oö-ALA will be formed o Pyridoxal phosphate (vit. B6) is a coenzyme for this reaction acd aardßf=k+öö$$, tsars ((iJh)
  11. Haemoglobin synthesis A series of biochemical reactions will follow Two molecules of ö-ALA condense form a pyrrole called porphobilinogen (PBG) Four PBG condense to form a tetrapyrrole uroporphyrinogen Ill. UPG Ill is then converted to coproporphyrinogen CPG then changes to protoporphyrin which ultimately combines with irc in the ferrous state (Fe2+) to form haem acd Bf Pr.&prpyn tars ((iJh) 0
  12. HAEMOGLOBIN SYNTHESIS oEach molecule of haem combines with a globin chain. OA tetramer of four globin chains oeach with its own haem group formed to make up a haemoglobin molecule
  13. Function of haemoglobin Olt facilitates oxygen transport Olt facilitates carbondioxide alt has important role as a buffer. alt transport NO
  14. HAEMOGLOBIN OXYGEN BINDING oOne Hb can bind to four 02 molecules dess than .01 sec required for oxygenation oß chain move closer when oxygenated oWhen oxygenated 2,3-DPG is pushed out oß chains are pulled apart when 02 is unloaded, o permitting entry of 2,3-DPG resulting in lower affinity of 02
  15. Oxy Oxyhaemoglobin Deoxyhaemoglobin
  16. Oxygen-haemoglobin dissociation curve 002 carrying capacity of Hb at different P02 oSigmoid shape 0Binding of one molecule facilitate the second molecule binding •P 50 (partial pressure of 02 at which Hb is half saturated with 02) 26.6mmHg
  17. Hb-oxygen dissociation curve Hb 02 100 80 60 20 o o Hb F 2,3-DPGU pH T 20 2 2,3-DPGt pH U 60 arterial 1 00 (mmHg) 4 40 6 80 8 10 12 14 (kPa) partial pressure of oxygen
  18. OXYGEN DISSOCIATION CURVE 0The normal position of curve depends on oConcentration of 2,3-DPG OH + ion concentration (pH) OC02 in red blood cells oStructure of Hb
  19. ABNORMAL HAEMOGLOBIN SICKLE CELL ANEMIA is related disorder Inherited autosomal disease Replacement of glutamate residue By valine at position 6 in the ß —chain Hb reacts to deoxigenated & dehydration By solidifying and stretching the erythrocytes Elongated shape of RBC More pronoun in homozygous condition Normal rcd blood cell formation of sicklcd rcd blood cell Sickled red blood cell
  20. Sickle cell anemia Normal GGÅ CT C CTC Partial RNA GAG GAG Missense Mutation GGA CTC CCU GUG GAG
  21. THANK YOU REFRENCE VIEWS REVIEWS GANONGS PATH FINDER GRAPHS FROM NET

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