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TAMU BICH 410 - Hemoglobin
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FBICH 410 1st Edition Lecture 13Outline of Last Lecture - Myoglobin- HemoglobinOutline of Current Lecture - Hb T to Ro 1st binding low affinity To 2nd binding T to Ro 3rd binding high affinity R o 4th high affinity R- Cooperativity is designed to release O2 at low pressures- Y= pO2n/p50n+pO2n- Allosteric effects- binding of one site affects another siteo Hb is allosteric quaternary proteino Homotropic- ligand and effector identicalo Heterotropic- “”” differento Binding of something that lowers O2 affinity increases p50 and moves curve to the right-T STATEo Binding of something that increases O2 affinity decreases p50 and moves curve to left- R stateo Bohr effect- binding of O2 decreases proton bindingo Bohr effect- pka of ionizable groups in ionic interactions are perturbed- specifically His146 DeoxyHb- T state- favors ionic interactions to form stable structure therefore protonated oxyHb- R state- O2 binds and ionic interactions disrupted- deprotonated- High H favors protonation- favors T state lowers O2 affinity and increases p50- CO2 allosteric effector- diminishes O2 binding decreasing pH and Hb acts as CO2 transporter- Carbonic Anhydrase- C02 +H20 H+ +HCO3-o Carbonic anhydrase accelerates rxno CO2 lowers the pH of bloodo O2 depleted and muscles make lactic acid lowering pHo Consequently protons are taken up by Hb as O2 dissociates- Carbamation- Hb acts as CO2 transportero HCO3- binds to amino N terminal group and forms carbamateso Aids in transport of CO2 to lungso Increases Bohr effect by releasing H+These notes represent a detailed interpretation of the professor’s lecture. GradeBuddy is best used as a supplement to your own notes, not as a substitute.o Carbamates form ion pairs and stabilize deoxy- Allosteric- shift to T release O2 (co2, bpg, h+) and shift to r state bind O2- 02 favors R state and releases H+ causing equilibrium to CO2 to H20 SO c02 can be expired- Hb releases 02- CO2 abundant pH low- favors deoxy state - BPG- reason why O2 binds tighter to pure Hb than serumo Binds to central cavity of deoxyHb- has -5 charge which interacts with positive charge amino acids in Hb- Decreases O2 and pressure with altitude- increases BPG production so increases O2 delivered to tissues- Fetal Hb- fetus receives O2 from mothers blood via placentao Fetal blood has higher affinity for O2 than mothero HbF has composition alpha2gamma2o HbF has lower affinity for BPG than HbAo Differences accounted for Ser 143 in place of His 143 in


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TAMU BICH 410 - Hemoglobin

Type: Lecture Note
Pages: 2
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