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. 1979 Aug 15;182(2):617–619. doi: 10.1042/bj1820617

An active-site-directed adenosine triphosphate analogue binds to the beta-subunits of factor F1 mitochondrial adenosine triphosphatase with its triphosphate moiety.

V L Drutsa, I A Kozlov, Y M Milgrom, Z A Shabarova, N I Sokolova
PMCID: PMC1161345  PMID: 159698

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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