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• W1558048696 abstract "The kinetic properties of sea urchin flagellar dynein ATPase have been reinvestigated using a continuous assay which regenerates ATP and contains P1,P5-di(adenosine-5')pentaphosphate, a potent adenylate kinase inhibitor. Earlier studies (Shimizu, T. (1981) Biochemistry 20, 4347-4354) revealed complex, highly cooperative kinetics with respect to MgATP2- concentration in the absence of this inhibitor. With Ap5A, the kinetics are characteristic of classical Michaelis-Menten enzymes. Isolated 21 S and 14S enzyme forms were also examined, and their kinetic parameters are presented Vanadate inhibition patterns in the presence of P1,P5-di(adenosine-5')pentaphosphate lose their nonlinear character, and we observe linear noncompetitive inhibition of the mixed type." @default.
• W1558048696 created "2016-06-24" @default.
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• W1558048696 creator A5054730579 @default.
• W1558048696 date "1982-06-01" @default.
• W1558048696 modified "2023-09-26" @default.
• W1558048696 title "A reinvestigation of dynein ATPase kinetics and the inhibitory action of vanadate." @default.
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• W1558048696 doi "https://doi.org/10.1016/s0021-9258(18)34478-8" @default.
• W1558048696 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/6211437" @default.
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