| Autor: |
Drutsa, V L, Kozlov, I A, Milgrom, Y M, Shabarova, Z A, Sokolova, N I |
| Zdroj: |
Biochemical Journal; August 1979, Vol. 182 Issue: 2 p617-619, 3p |
| Abstrakt: |
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. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
|
