[天然α-辅肌动蛋白的有限胰蛋白酶水解片段]
[Fragments of limited trypsinolysis of native alpha-actinin].
作者信息
Simonidze M Sh, Kuridze K Sh, Nadirashvili N Sh, Zaalishvili M M
出版信息
Bioorg Khim. 1985 Nov;11(11):1493-6.
PMID:4091862
Abstract
Incubation of native alpha-actinin with trypsin leads to the formation of intermediate fragments that are quite resistant to further enzyme action (M 98, 85, 80, 70, 64, 55, 38, 30, 15 kDa). Analysis of these fragments made it possible to elucidate the course of trypsinolysis and to localize the fragments in the polypeptide chain of alpha-actinin subunit.
摘要
将天然α-辅肌动蛋白与胰蛋白酶一起温育会导致形成对进一步酶作用相当有抗性的中间片段（分子量为98、85、80、70、64、55、38、30、15 kDa）。对这些片段的分析使得阐明胰蛋白酶消化过程并将片段定位在α-辅肌动蛋白亚基的多肽链中成为可能。
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