Abstract:
:Since one of the electrophysiological effects of pyrithiamin, an antimetabolite of thiamin, suggested an interference with sodium pump mechanisms, the effect of pyrithiamin on Na+,K+-ATPase was investigated. We found that whereas preincubation of the antimetabolite with nonneuronal preparations of Na+,K+-ATPase produced only minimal inhibition, the enzyme derived from brain preparations was markedly inhibited. This inhibition could be prevented by thiamin but not reversed. The kinetic study showed that pyrithiamin acts in a noncompetitive manner with respect to the activation of the enzyme by ATP, Na+, and K+. Pyrithiamin inhibited Na+-dependent phosphorylation and K+-stimulated phosphatase as well as ouabain binding, and these inhibitions were parallel with that of the overall Na+,K+-ATPase reaction. In addition, the antimetabolite caused a significant change in the turbidity of the enzyme suspension. The results suggest that pyrithiamin may induce a structural change of the enzyme complex.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Matsuda T,Cooper JRdoi
10.1021/bi00278a023subject
Has Abstractpub_date
1983-04-26 00:00:00pages
2209-13issue
9eissn
0006-2960issn
1520-4995journal_volume
22pub_type
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