绒泡菌肌动蛋白结合蛋白的分离与鉴定。

Isolation and characterization of Physarum profilin.

作者信息

Ozaki K, Sugino H, Hasegawa T, Takahashi S, Hatano S

出版信息

J Biochem. 1983 Jan;93(1):295-8. doi: 10.1093/oxfordjournals.jbchem.a134167.

DOI:10.1093/oxfordjournals.jbchem.a134167

Abstract

A protein that functionally resembles mammalian and Acanthamoeba profilins, has been purified from Physarum plasmodia. Physarum profilin consists of a single polypeptide with a molecular weight of 11,000-13,000. It has an isoelectric point of 5.35-5.40 under denaturing conditions. The amino acid composition of this protein is similar to those of profilins isolated from other sources. Physarum profilin prolongs the process of actin polymerization in a concentration-dependent fashion. This effect is much stronger for Physarum G-actin than for muscle G-actin.

摘要

从黏菌原质团中纯化出了一种在功能上类似于哺乳动物和棘阿米巴肌动蛋白单体结合蛋白的蛋白质。黏菌肌动蛋白单体结合蛋白由一条分子量为11,000 - 13,000的单一多肽组成。在变性条件下，其等电点为5.35 - 5.40。这种蛋白质的氨基酸组成与从其他来源分离出的肌动蛋白单体结合蛋白相似。黏菌肌动蛋白单体结合蛋白以浓度依赖的方式延长肌动蛋白聚合过程。这种效应在黏菌球形肌动蛋白上比在肌肉球形肌动蛋白上要强得多。