ACTIVE-SITE-DIRECTED ADENOSINE-TRIPHOSPHATE ANALOG BINDS TO THE BETA-SUBUNITS OF FACTOR-F1 MITOCHONDRIAL ADENOSINE-TRIPHOSPHATASE WITH ITS TRIPHOSPHATE MOIETY

被引：30

作者：

DRUTSA, VL ^{[1
]}

KOZLOV, IA ^{[1
]}

MILGROM, YM ^{[1
]}

SHABAROVA, ZA ^{[1
]}

SOKOLOVA, NI ^{[1
]}

机构：

[1] MV LOMONOSOV STATE UNIV, BELOZERSKII MOLEC BIOL & BIOORGAN CHEM LAB, DEPT BIOENERGET, MOSCOW 117234, USSR

来源：

BIOCHEMICAL JOURNAL | 1979年 / 182卷 / 02期

关键词：

D O I：

10.1042/bj1820617

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：

The reaction of the mixed anhydride of [3H]ATP and mesitylenecarboxylic acid and soluble mitochondrial adenosine triphosphatase is accompanied by the covalent binding of one molecule of the inhibitor to a molecule of the enzyme and results in the inhibition of adenosine triphosphatase activity by more than 90%. The electrophoresis of adenosine triphosphatase modified by reaction with the mixed anhydride of [3H]ATP and mesitylenecarboxylic acid in polyacrylamide gel in the presence of sodium dodecyl sulphate showed that the inhibitor is bound to the beta-subunit of the enzyme. The results suggest that ATP may also bind to the beta-subunit of the adenosine triphosphatase with its triphosphate moiety.

引用

页码：617 / 619

页数：3

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