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: 3287273
• 负责人: JAMES R BAMBURG
• 金额: $ 12.73万
• 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/3287273
• 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.

根据 G-肌动蛋白抑制水解的能力进行检测 DNAase 的活性，我们从大脑中分离出一种蛋白质，它可以主动 促进溶液中 F-肌动蛋白的解聚。 该蛋白质现在将是 进一步表征其分子量、等电点、氨基酸 成分及其与单独的 F-肌动蛋白和存在时相互作用的能力 相关蛋白，如原肌球蛋白。 DNAase 抑制测定的改进已被开发出来，允许 在无 F-肌动蛋白存在的条件下进行 G-肌动蛋白测定 两个肌动蛋白池之间发生交换。 该测定将应用于 同步化 CHO 细胞中 G 和 F 肌动蛋白浓度的测量 细胞周期。