Vanadium-51 NMR study of vanadate binding to myosin and its subfragment 1

作者: Israel Ringel , Y. Michael Peyser , Andras Muhlrad

DOI: 10.1021/BI00490A029

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摘要: The binding of various forms vanadate to myosin and subfragment 1 (S-1) was studied by {sup 51}V NMR at increasing concentrations between 0.06 1.0 mM. distribution the in solution depended on total concentration vanadate. At low concentrations, predominant form monomeric, while high concentration, it tetrameric. presence or S-1 produced a significant broadening signal each vanadate, indicating that all them bind proteins. Addition ATP, which does not affect spectra absence proteins, causes their alteration S-1. changes, include monomeric narrowing oligomeric forms, indicate more less binds proteins than ATP. Irradiation near-UV light cleaves three specific sites-at 23, 31, 74 kDa from N-terminus. cleavages 23 31 are specifically inhibited themore » addition vanadate-associated photocleavage also depends vanadate; is observed only when least 0.2 This lowest detected spectra. From parallel dependence appearance tetrameric concluded occurs S-1.« less

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