DYNAMICS OF ACTIN FILAMENTS IN NERVE GROWTH

肌动蛋白丝在神经生长中的动力学

• 批准号: 3287279
• 负责人: JAMES R BAMBURG
• 金额: $ 13.76万
• 依托单位: COLORADO STATE UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 1984
• 资助国家: 美国
• 起止时间: 1984-12-01 至 1989-11-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/3287279
• 关键词: adenosinetriphosphatase; affinity chromatography; autoradiography; brain; brain metabolism; cell growth regulation; cell population study; circular dichroism; conformation; density gradient ultracentrifugation; electrofocusing; electron microscopy; gel electrophoresis; glia; ions; local anesthetics; messenger RNA; neuropharmacology; neurotrophic factors; stoichiometry; tissue /cell culture; ultraviolet spectrometry; wheat

Using an assay for G-actin based on its ability to inhibit the hydrolytic activity of DNAase, we have isolated a protein from brain which actively promotes the depolymerization of F-actin in solution. This protein will now be further characterized as to its molecular weight, isoelectric point, amino acid composition and its ability to interact with F-actin alone and in the presence of associated proteins such as tropomyosin. A modification of the DNAase inhibition assay has been developed which permits the assay of G-actin in the presence of F-actin under conditions where no exchange between the two actin pools occurs. This assay will be applied to the measurement of G and F-actin concentrations in synchronized CHO cells during the cell cycle.

使用基于G-肌动蛋白抑制蛋白水解的能力的G-肌动蛋白测定法， 为了研究DNA酶的活性，我们从脑中分离出一种蛋白质， 促进溶液中F-肌动蛋白的解聚。 这种蛋白质现在将 进一步表征其分子量、等电点、氨基酸 本发明的组合物及其与单独的F-肌动蛋白和在存在下的F-肌动蛋白相互作用的能力， 相关蛋白质如原肌球蛋白。 已经开发了DNA酶抑制测定的修改，其允许 在F-肌动蛋白存在的条件下，G-肌动蛋白的测定， 两个肌动蛋白池之间发生交换。 本试验将应用于 同步化CHO细胞中G和F-肌动蛋白浓度的测量 细胞周期