Nonequivalence of chains in hemoglobin oxidation and oxygen binding. Effect of organic phosphates
A Mansouri, KH Winterhalter - Biochemistry, 1974 - ACS Publications
A Mansouri, KH Winterhalter
Biochemistry, 1974•ACS PublicationsOxidation of Hb A is governed by at least two fac-tors:(a) the intrinsic susceptibility to
oxidation of chains which depend on their primary structure, and (b) the affinity of chains for
oxygen or other ligands. 2, 3-Diphosphoglycerate (2, 3-DPG) stabilizesthe deoxy
conformationof hemoglobin which has a lower affinity for oxygen. This effect is maximal at
acid and minimal at alkaline pH. Hemoglobin F| which does not bind organic
phosphatesdoes not show significant affinity
oxidation of chains which depend on their primary structure, and (b) the affinity of chains for
oxygen or other ligands. 2, 3-Diphosphoglycerate (2, 3-DPG) stabilizesthe deoxy
conformationof hemoglobin which has a lower affinity for oxygen. This effect is maximal at
acid and minimal at alkaline pH. Hemoglobin F| which does not bind organic
phosphatesdoes not show significant affinity
Abstract
Oxidation of Hb A is governed by at least two fac-tors:(a) the intrinsic susceptibility to oxidation of chains which depend on their primary structure, and (b) the affinity of chains for oxygen or other ligands. 2, 3-Diphosphoglycerate (2, 3-DPG) stabilizesthe deoxy conformationof hemoglobin which has a lower affinity for oxygen. This effect is maximal at acid and minimal at alkaline pH. Hemoglobin F| which does not bind organic phosphatesdoes not show significant affinity
ACS Publications