ENDORPHIN, PHENOTHIAZINE AND ENZYME SITES ON CALMODULIN

钙调蛋白上的内啡肽、吩噻嗪和酶位点

• 批准号: 3288111
• 负责人: J DAVID PUETT
• 金额: $ 22.21万
• 依托单位: UNIVERSITY OF MIAMI SCHOOL OF MEDICINE
• 依托单位国家: 美国
• 财政年份: 1985
• 资助国家: 美国
• 起止时间: 1985-08-30 至 1988-07-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/3288111
• 关键词: calcium; chemical binding; conformation; electron spin resonance spectroscopy; high performance liquid chromatography; lysine; phenothiazines; phosphodiesterases; phosphorylase kinase; vanadium

The proposed research represents an integrated chemical and physicochemical approach to elucidate the molecular parameters involved in the association of calmodulin with Beta-endorphin, phenothiazines, phosphodiesterase, calcium and vanadyl. Direct binding studies of endorphin and phenothiazines will be conducted to pursue the nature of the cooperativity that has been observed. Chemical studies will focus on differential trace labeling to assess individual lysine reactivities in calmodulin as influenced by the various ligands. A feasibility study will be undertaken using a novel technique for identification of the endorphin binding sites on calmodulin and the regions. Considerable effort will be devoted to ESR spectroscopy of spin labeled calmodulin and vanadyl-calmodulin complexes, several probes will be used to modify calmodulin, and spin labeled chlorpromazine-calmodulin complexes will be investigated. These studies should provide useful information on the mechanisms by which calmodulin can associate with a variety of simple ligands and complex enzymes.

拟议的研究代表了综合的化学和物理化学 方法来阐明参与关联的分子参数 β-内啡肽，吩噻嗪，磷酸二酯酶， 钙和氧钒。 内啡肽与 吩噻嗪类化合物将被用来研究协同效应的性质 这是观察到的。 化学研究将侧重于微分跟踪 标记以评估钙调蛋白中的单个赖氨酸反应性， 受到各种配体的影响。 将进行可行性研究 使用一种新的技术来鉴定内啡肽结合位点 对钙调素和区域的影响。 政府会致力进行外判工作 自旋标记的钙调蛋白和钒酰-钙调蛋白复合物的光谱学， 将使用几种探针来修饰钙调素，并自旋标记 将研究氯丙嗪-钙调蛋白复合物。 这些研究 应该提供有用的信息，钙调蛋白的机制， 与各种简单配体和复杂酶结合。