Tam J W, Cheng L Y
Biochim Biophys Acta. 1979 Sep 29;580(1):75-84. doi: 10.1016/0005-2795(79)90198-3.
Native and reconstituted hemoglobin H molecules were cross-linked with glutaraldehyde at pH values close to the physiological. The Schiff base adducts were analysed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis before and after reduction with sodium borohydride. The major component had a molecular weight of about 31 000 which corresponded to the dimeric species of the beta subunit. In contrast to the native protein, which has very high oxygen affinity and no heme-heme interaction or 2,3-diphosphoglyceric acid effect, the modified hemoglobin H molecules showed cooperative oxygen binding, decreased oxygen affinity and a noticeable 2,3-diphosphoglyceric acid effect.
天然和重组的血红蛋白H分子在接近生理pH值的条件下与戊二醛交联。在用硼氢化钠还原前后，通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳分析席夫碱加合物。主要成分的分子量约为31000，对应于β亚基的二聚体形式。与具有非常高的氧亲和力且不存在血红素-血红素相互作用或2,3-二磷酸甘油酸效应的天然蛋白质不同，修饰后的血红蛋白H分子表现出协同氧结合、降低的氧亲和力和显著的2,3-二磷酸甘油酸效应。
