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: 3288116
• 负责人: J DAVID PUETT
• 金额: $ 24.05万
• 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 1989-12-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/3288116
• 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.

拟议的研究代表了一项综合的化学和物理化学研究。 阐明相关分子参数的方法 钙调蛋白与β-内啡肽、吩噻嗪、磷酸二酯酶、 钙和钒。内啡肽和内啡肽的直接结合研究 将进行吩噻嗪类药物的研究，以追求协同作用的本质 这一点已经被观察到了。化学研究将集中在差示踪迹上 钙调素AS中单个赖氨酸反应性的标记评估 受各种配体的影响。将进行可行性研究 用一种新的技术鉴定内啡肽结合位点 关于钙调蛋白和这些区域。将在ESR方面投入相当大的努力 自旋标记的钙调蛋白和钒-钙调蛋白络合物的光谱， 几个探针将被用来修饰钙调蛋白，并自旋标记 氯丙嗪-钙调蛋白复合体将被研究。这些研究 应提供有关钙调蛋白通过何种机制 与多种简单的配体和复杂的酶结合。

项目成果

Interaction of alpha-N-Acetyl-beta-endorphin and calmodulin.

α-N-乙酰-β-内啡肽和钙调蛋白的相互作用。

• DOI: 10.1007/bf01025412
• 发表时间: 1988
• 期刊: Journal of protein chemistry
• 作者: Lovegren,ES;Ling,N;Puett,D
• 通讯作者: Puett,D

Vanadium (IV) inhibits calmodulin-stimulated skeletal muscle myosin light chain kinase activity.

钒 (IV) 抑制钙调蛋白刺激的骨骼肌肌球蛋白轻链激酶活性。

• 发表时间: 1995
• 期刊: BioFactors (Oxford, England)
• 作者: Parra-Diaz,D;Echegoyen,L;Zot,HG;Puett,D
• 通讯作者: Puett,D

Binding of amphiphilic peptides to a carboxy-terminal tryptic fragment of calmodulin.

两亲性肽与钙调蛋白的羧基末端胰蛋白酶片段的结合。

• DOI: 10.1021/bi00417a006
• 发表时间: 1988
• 期刊: Biochemistry
• 影响因子: 2.9
• 作者: Sanyal,G;Richard,LM;Carraway3rd,KL;Puett,D
• 通讯作者: Puett,D

Fluorescent adducts of wheat calmodulin implicate the amino-terminal region in the activation of skeletal muscle myosin light chain kinase.

小麦钙调蛋白的荧光加合物表明氨基末端区域参与骨骼肌肌球蛋白轻链激酶的激活。

• 发表时间: 1990
• 期刊: The Journal of biological chemistry
• 作者: Zot,HG;Aden,R;Samy,S;Puett,D
• 通讯作者: Puett,D

Electron spin resonance of calmodulin-vanadyl complexes.

钙调蛋白-氧钒复合物的电子自旋共振。

• DOI: 10.1021/bi00388a053
• 发表时间: 1987
• 期刊: Biochemistry
• 影响因子: 2.9
• 作者: Nieves,J;Kim,L;Puett,D;Echegoyen,L;Benabe,J;Martinez-Maldonado,M
• 通讯作者: Martinez-Maldonado,M