Poyart C, Girard F, Bursaux E, Bohn B
Ann Biol Clin (Paris). 1981;39(4):213-22.
Functional properties of tetrameric HbA are schematically described in this short review. After considering the various structures of the protein and its binding with heme, an attempt is made to explain the influence of this structure on the affinity of Hb for oxygen, cooperative binding of oxygen, and the alkaline Bohr effect. Fixation of erythrocytic anions (chlorine and 2,3 diphosphoglycerate) modulate certain intrinsic properties, allowing the Hb molecule to provide for efficacious transport of oxygen between the environment and the metabolically active tissues.
本简短综述概要描述了四聚体血红蛋白A（HbA）的功能特性。在考虑了该蛋白质的各种结构及其与血红素的结合后，我们尝试解释这种结构对Hb与氧的亲和力、氧的协同结合以及碱性玻尔效应的影响。红细胞阴离子（氯离子和2,3-二磷酸甘油酸）的固定调节了某些内在特性，使Hb分子能够在环境与代谢活跃组织之间有效地运输氧气。
