Drutsa, V L;
Kozlov, I A;
Milgrom, Y M;
Shabarova, Z A;
Sokolova, N I
An active-site-directed adenosine triphosphate analogue binds to the β-subunits of factor F1 mitochondrial adenosine triphosphatase with its triphosphate moiety
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Media type:
E-Article
Title:
An active-site-directed adenosine triphosphate analogue binds to the β-subunits of factor F1 mitochondrial adenosine triphosphatase with its triphosphate moiety
Contributor:
Drutsa, V L;
Kozlov, I A;
Milgrom, Y M;
Shabarova, Z A;
Sokolova, N I
Published:
Portland Press Ltd., 1979
Published in:
Biochemical Journal, 182 (1979) 2, Seite 617-619
Description:
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.