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 饱和的配体，如氧或一氧化碳，配体亲和力 未反应的血红素基团的比例增加。这需要一种类型的 这些血红素群体之间的交流。这就是我们的目标 调查以了解这一事件和其他相关事件的分子基础 血红蛋白中的变构现象。不同组件的功能属性 分子的结构状态将被确定，并且序列 伴随着分子与配体饱和的结构变化 探索过了。将利用鲤鱼探索血红蛋白的结构转变 作为模型体系的血红蛋白在这个分子中的变化是三级的 PH和有机磷浓度的变化可以诱导结构 而与血红素基团的配位状态无关。 与血红素上单一位点发生反应的抗体群体的特性 将探索蛋白质抗原和平衡常数和动力学常数 它们与其特定抗原的反应是在各种不同的 条件。这种位点特异性抗体将被用作结构蛋白的探针 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.