[从脊髓灰质炎病毒中分离纯化3C蛋白酶。鉴定该酶的活性形式]
[Isolation and purification of 3C-proteinase from the poliomyelitis virus. Identification of an active form of the enzyme].
作者信息
Sablina E P, Antonov V K
出版信息
Bioorg Khim. 1991 Sep;17(9):1213-22.
PMID:1666950
Abstract
All the forms of 3C protease previously found were isolated and purified. A 3D polymerase's fragment covalently bound with 3C protein does not affect the specific proteolytic activity of the enzyme, whereas the elimination of 26 N-terminal amino acid residues of 3C protease leads to its inactivation.
摘要
先前发现的所有形式的3C蛋白酶均被分离和纯化。与3C蛋白共价结合的3D聚合酶片段不会影响该酶的特异性蛋白水解活性，而去除3C蛋白酶的26个N端氨基酸残基会导致其失活。
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