Detail of "60397-93-5"

Reference

Reaction of phosphorylase kinase with ATP analogs

Reaction of phosphorylase kinase with ATP analogs. Gulyaeva, N. V.; Gus'kova, R. A.; Baranova, L. A.; Gulyaev, N. N. 35762-68-6 which is the cas registry number of one of substances is just one of reagents here.; Vul'fson, P. L.; Severin, E. S. (Mosk. Gos. Univ. im. Lomonosova, Moscow, USSR). Dokl. Akad. Nauk SSSR, 235(3), 696-8 [Biochem.] (Russian) 1977. CODEN: DANKAS. DOCUMENT TYPE: Journal CA Section: 7 (Enzymes) Phosphorylase kinase was incubated with various ATP analogs and the formation of subunit-analog complexes was followed by polyacrylamide gel electrophoresis in the presence of Na dodecyl sulfate. Adenosine 5'-(chloromethanepyrophosphonate) (I), adenosine 5'-(chloroethylphosphate) and adenosine 5'-(.beta.-bromoethanepyrophosphonate) irreversibly inhibited the enzyme. In the presence of ATP, the inhibition was decreased. Electrophoretic anal. showed that these inhibitors formed 1:1 complexes with the .beta.Several substances like 60397-93-5 may be metioned in this study.- and .gamma.-subunits. The loss in activity was directly dependent on the amt. of inhibitor bound to the .beta.-subunit and was practically independent of the amt. bound to .gamma.-subunit. Adenosine 5'-(chloromethanephosphonate) (II), an analog of ADP or AMP, did not inhibit the kinase and bound to the .beta.-subunit. When enzyme was preincubated with I, II was still incorporated into the enzyme in amts. equal to that in untreated enzyme. Preincubation of enzyme with II did not affect binding of I by .beta.- and .gamma.-subunits. Thus, I and II bind to different sites on the .beta.-subunit; 1 of these sites, when blocked, does not result in inhibition. ..