ENZYMOLOGICAL ASPECTS OF NEURAL FUNCTION

神经功能的酶学方面

• 批准号: 4696775
• 负责人: R WAYNE ALBERS
• 金额: --
• 依托单位: NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE
• 依托单位国家: 美国
• 资助国家: 美国
• 起止时间: 至
• 项目状态: 未结题
• 来源: https://reporter.nih.gov/project-details/4696775
• 关键词: adenosinetriphosphatase; aquatic organism; autoradiography; bioenergetics; brain metabolism; complementary DNA; conformation; enzyme structure; gel electrophoresis; hydrolysis; isozymes; membrane potentials; messenger RNA; monoclonal antibody; neurochemistry; nucleic acid sequence; phosphorylation

This project comprises an invstigation of the structure and functioning of the sodium pump. Rapid quenching studies have shown the presence of an "intermediate" component of the dephosphorylation rate curve in the membrane-bound enzyme from Electophorus electric organ. We have developed two different preparations of soluble Na,K-ATPase. One of these preserves the membrane-type dephosphorylation kinetics, whereas the other type displays monophasic dephosphorylation. Disappearance of the intermediate rate component is correlatd with a doubling of catalytic activity. Since molecular seiving and cross-linking studies indicate that both preparations consist of monodisperse associations of 3-4 enzyme protomers, the provisional hypothesis for current studies is that the native enzyme exists as an oligomer and that modification of oligomeric interactions by the solubilizing detergent is responsible for the altered kinetics. Other studies to correlate these differences with physical and other biochemical parameters of the Na,K-ATPase and to determine the transport competence of the two forms are in progress.

该项目包括对结构和功能的发明 钠泵。 快速淬火研究表明存在 去流磷酸化率曲线的“中间”成分 来自电力器官的膜结合酶。 我们已经发展了 可溶性Na，K-ATPase的两种不同的制剂。 这些保留之一 膜型去磷酸化动力学，而另一种类型 显示单相去磷酸化。 中级消失 速率成分与催化活性增加一倍相关。 自从 分子观察和交联研究表明，两种制剂 由3-4个酶原子的单分散关联组成， 当前研究的临时假设是存在天然酶 作为低聚物，并通过 溶解洗涤剂会导致动力学改变。 其他 将这些差异与物理和其他生化的研究相关 Na，K-ATPase的参数并确定运输能力 这两种形式正在进行中。