英文课件-血红蛋白和抗体.pptVIP

Biochemistry Hemoglobin and Immunoglobulins Myoglobin (p49 fig 7-3) Structure of Myoglobin a single polypeptide chain of 153 amino acids a single heme group in a hydrophobic pocket 8 regions of ?-helix; no regions of ?-sheet most polar side chains are on the surface nonpolar side chains are folded to the interior two His side chains are in the interior, involved with interaction with the heme group Fe(II) of heme has 6 coordinates sites; 4 interact with N atoms of heme, 1 with N of a His side chain, and 1 with either an O2 molecule or an N of the second His side chain Heme structure P49 Figure 7-4 Hemoglobin Oxygen Binding of Hb a tetramer of two ?-chains (141 amino acids each) and two ?-chains (153 amino acids each); a2b2 each chain has 1 heme group; hemoglobin can bind up to 4 molecules of O2 binding is cooperative; when one O2 is bound, it becomes easier for the next O2 to bind the function of hemoglobin is to transport oxygen the structure of oxygenated Hb is different from that of unoxygenated Hb H+, CO2, Cl-, and 2,3-bisphosphoglycerate (BPG) affect the ability of Hb to bind and transport oxygen Oxygen Binding of Hb P51 Fig7-8 : O2 binding of hemoglobin and myoglobin Cooperativity of Binding/Release The oxygenation state (filled or empty) of one site of the multisubunit hemoglobin can be communicated to another site, resulting in cooperative binding and release of oxygen. —— Allosteric binding Oxygen Binding of Hb The effect of pH on the oxygen-binding ability of Hb is called the Bohr effect (p53 fig7-16) as pH decreases (more acidic), oxygen is released CO2 promotes release of O2 from HbO2 Oxygen Binding of Hb Figure The Bohr effect Oxygen Binding of Hb Table Summary of the Bohr effect Hemoglobin (Hb) Hemoglobin in blood is bound to BPG interaction is electrostatic, between negative charges on BPG(2,3-bisphosphoglycerate,