Drutsa V L, Kozlov I A, Milgrom Y M, Shabarova Z A, Sokolova N I
Biochem J. 1979 Aug 15;182(2):617-9. doi: 10.1042/bj1820617.
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.
[3H]ATP与均三甲苯羧酸的混合酸酐与可溶性线粒体腺苷三磷酸酶的反应伴随着一分子抑制剂与一分子酶的共价结合，并导致腺苷三磷酸酶活性被抑制90%以上。在十二烷基硫酸钠存在的情况下，对经[3H]ATP与均三甲苯羧酸的混合酸酐反应修饰的腺苷三磷酸酶进行聚丙烯酰胺凝胶电泳，结果表明抑制剂与该酶的β亚基结合。这些结果表明，ATP也可能以其三磷酸部分与腺苷三磷酸酶的β亚基结合。
