Proteolysis and structure of skeletal muscle actin.
Proteolysis and structure of skeletal muscle actin.
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骨骼肌肌动蛋白的蛋白水解和结构。
DOI：
10.1073/pnas.81.12.3680
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发表时间：
1984
影响因子：
11.1
通讯作者：
Ue,K
中科院分区：
文献类型：
--
作者：
Mornet,D;Ue,K
在标准条件下，G-肌动蛋白被提交给9种不同特异性的蛋白酶，每种情况下产生的片段模式都用NaDodSO4凝胶电泳法进行了研究。结果表明，肌动蛋白单体由一个大的区域(约33千道尔顿)和一个小的、易降解的区域(约9千道尔顿)组成。COOH的末端在大范围内。对初级序列同源性、肌动蛋白晶体的中分辨率图谱和肌动蛋白的某些反应的考虑表明，NH2末端位于较小的区域，二价金属阳离子通常被螯合到的负序列也是如此，但核苷酸结合位置在区域之间连接附近的较大区域。通过对这些结果的分析，肌动蛋白的许多性质是可以理解的。
Under standard conditions, G-actin has been submitted to nine proteases of varying specificity, and in each case the pattern of fragments produced has been studied by NaDodSO4 gel electrophoresis. The results suggest that the actin monomer consists of a large region (ca. 33 kilodaltons) and a small, easily degraded region (ca. 9 kilodaltons). The COOH terminus is in the large region. Consideration of primary sequence homologies, medium resolution maps of actin crystals, and certain reactions of actin suggests that the NH2 terminus is in the small region, as is the negative sequence to which a divalent metal cation is normally chelated, but that the nucleotide-binding site is on the large region near the junction between the regions. From analysis of these results, numerous properties of actin are understandable.