HALF-SITE AFFINITY MODIFICATION OF TRYPTOPHANYL-TRANSFER RNA-SYNTHETASE LEADS TO FREEZING OF THE FREE SUBUNIT

被引：15

作者：

FAVOROVA, OO ^{[1
]}

MADOYAN, IA ^{[1
]}

DRUTSA, VL ^{[1
]}

机构：

[1] MV LOMONOSOV STATE UNIV,MOSCOW 117234,USSR

来源：

FEBS LETTERS | 1981年 / 123卷 / 02期

关键词：

D O I：

10.1016/0014-5793(81)80277-3

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

引用

页码：161 / 164

页数：4

共 21 条

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[3]

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[4] ACTIVE-SITE TITRATION AND AMINOACYL ADENYLATE BINDING STOICHIOMETRY OF AMINOACYL-TRANSFER-RNA SYNTHETASES [J].

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[5] ANTI-COOPERATIVE BINDING OF L-TRYPTOPHAN TO TRYPTOPHANYL-TRNA SYNTHETASE FROM BEEF PANCREAS - STUDY AT EQUILIBRIUM BY DIALYSIS AND CHANGES IN SPECTROSCOPIC PROPERTIES [J].

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[8]

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[10]

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