REACTION OF HEMOGLOBIN WITH LIGANDS AND ANTIBODIES

随着血红蛋白分子的四个血红素基团逐渐变得 饱和配体，如氧或一氧化碳，配体亲和力 未反应的血红素基团的增加。 这就需要一种 这两个群体之间的联系。 这是我们的目标 调查，以了解这一点和其他相关的分子基础 血红蛋白的变构现象。 不同的功能特性 分子的结构状态将被确定， 伴随着配体饱和的分子的结构变化 探讨了 血红蛋白的结构转变将利用鲤鱼进行探索 血红蛋白作为模型系统，因为在这个分子中，三级结构的变化 结构可以通过pH和有机磷酸盐浓度的变化来诱导 而不管血红素基团的配位状态如何。 与血红素上单一位点反应的抗体群的性质 蛋白质抗原将被探索和平衡和动力学常数为 它们与它们的特异性抗原的反应在各种条件下测定， 条件 这样的位点特异性抗体将用作结构分析的探针。 血红蛋白分子表面的变化。

As the four heme groups of the hemoglobin molecule become progressively saturated with ligands, such as oxygen or carbon monoxide, the ligand affinity of the unreacted heme groups increases. This necessitates a type of communication between these heme groups. It is the objective of this investigation to understand the molecular basis for this and the other related allosteric phenomena in hemoglobin. The functional properties of the different structural states of the molecule will be determined and the sequence of structural changes that accompany the saturation of the molecule with ligand explored. The structural transition in hemoglobin will be explored using carp hemoglobin as a model system since in this molecule the change in tertiary structure can be induced by variations of pH and organic phosphate concentration regardless of the state of liganding of the heme groups. The properties of antibody populations that react with single sites on heme protein antigens will be explored and the equilibrium and kinetic constants for their reactions with their specific antigens determined under a variety of conditions. Such site specific antibodies will be used as probes of structural changes at the surface of the hemoglobin molecule.