Mejía O, León-Velarde F, Monge C
Universidad Peruana Cayetano Heredia, Dpto. de Ciencias Fisiológicas, Lima, Perú.
Comp Biochem Physiol B Biochem Mol Biol. 1994 Oct-Nov;109(2-3):437-41. doi: 10.1016/0305-0491(94)90026-4.
A strain of high-altitude chickens (Gallus gallus) with a high hemoglobin-oxygen affinity has been found in the Peruvian Andes. The purpose in this work was to investigate the relation of this high affinity with the allosteric regulation of the inositol hexaphosphate effector (IHP). The hemoglobin-oxygen affinity has been determined in phosphate-free hemoglobin solutions before and after the addition of IHP. The results showed that the addition of IHP to the phosphate-free hemoglobin solutions increased the affinity significantly less in the high-altitude chicken (26.3 Torr) than in the sea-level chicken (42.2 Torr) (P < 0.001). It was concluded that the high-affinity hemoglobin is probably dependent on a molecular change affecting the allosteric regulation, although a change in the intrinsic properties of the hemoglobin cannot be discarded.
在秘鲁安第斯山脉发现了一种具有高血红蛋白-氧亲和力的高原鸡（原鸡）品系。这项工作的目的是研究这种高亲和力与肌醇六磷酸效应物（IHP）变构调节之间的关系。在添加IHP之前和之后，已在无磷酸盐的血红蛋白溶液中测定了血红蛋白-氧亲和力。结果表明，在无磷酸盐的血红蛋白溶液中添加IHP后，高原鸡（26.3托）的亲和力增加幅度明显小于海平面鸡（42.2托）（P < 0.001）。得出的结论是，高亲和力血红蛋白可能依赖于影响变构调节的分子变化，尽管不能排除血红蛋白内在特性的变化。
