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[胰蛋白酶对快肌肌球蛋白A-1轻链的片段化作用]

[Fragmentation of myosin A-1 light chain of fast muscle by trypsin].

作者信息

Cardinaud R

出版信息

C R Seances Acad Sci D. 1979 May 21;288(19):1481-4.

PMID:113121
Abstract

Limited proteolysis of myosin by such proteolytic enzymes as trypsin, chymotrypsin or papain produces typical fragmentation of its heavy chain. Presently evidence is given that trypsin treatment cleaves the alkali light chain A-1 (20,700 dalton) to a shorter (ca 20,000 dalton) chain. The two "essential" thiols (SH-1 and 2) of moysin were alkylated with 17-C-N-ethylmaleimide and a non-negligible amount of radioactivity was also found in the two alkali light chains. Using the specific radioactivity of alkali light chain A-1 it was possible to identify it among heavy chain fragmentation products. The molecular weight of the newly formed A-1 indicates that limited tryptic cleavage of this A-1 confers on it a closer similarity with alkali light chain A-2.

摘要

用胰蛋白酶、胰凝乳蛋白酶或木瓜蛋白酶等蛋白水解酶对肌球蛋白进行有限的蛋白水解会导致其重链出现典型的断裂。目前有证据表明,胰蛋白酶处理会将碱性轻链A-1(20,700道尔顿)切割成一条较短的(约20,000道尔顿)链。肌球蛋白的两个“必需”巯基(SH-1和2)用17-C-N-乙基马来酰亚胺进行了烷基化,并且在两条碱性轻链中也发现了不可忽略量的放射性。利用碱性轻链A-1的比放射性,有可能在重链断裂产物中识别出它。新形成的A-1的分子量表明,对这种A-1进行有限的胰蛋白酶切割使其与碱性轻链A-2有更密切的相似性。

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