ENZYMOLOGICAL ASPECTS OF NEURAL FUNCTIONS

神经功能的酶学方面

• 批准号: 6290606
• 负责人: ROBERT W 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/6290606
• 关键词: active sites; calmodulin dependent protein kinase; cations; chemical kinetics; enzyme activity; enzyme mechanism; enzyme structure; ion transport; mass spectrometry; neurochemistry; osmosis; phosphorylation; posttranslational modifications; protein structure function; sodium potassium exchanging ATPase; solvents; water

The principal study within this project concerns the transient kinetics of the sodium pump. A collaboration with J. Froehlich of NIA is directed at determining the extent to which oligomeric interactions of the sodium pump contribute to the efficiency of cation transport. We have obtained evidence, by a variety of techniques, that out-of-phase interactions of two or more alpha subunits occur in the native state of this and other P-type cation pumps. In addition, R. Wayne Albers is collaborating with P. Sharma and N. Amin of the LNC in studies of the mechanism of the cdk5 kinase reaction and the kinetics of the interaction of this kinase with its activator. - Na,K-ATPase sodium pump transient kinetics oligomeric interactions

该项目中的主要研究涉及钠泵的短暂动力学。与NIA的J. Froehlich进行的合作旨在确定钠泵的低聚相互作用在多大程度上有助于阳离子运输的效率。我们通过多种技术获得了证据表明，在该和其他P型阳离子泵的天然状态下发生了两个或多个α亚基的相位外相互作用。此外，R。WayneAlbers在研究CDK5激酶反应机理的研究和该激酶与其激活剂的相互作用的动力学方面与LNC的P. Sharma和N. Amin合作。 -NA，K-ATPase钠泵瞬态动力学寡聚相互作用