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Title: A dynein ATPase inhibitor isolated from a commercial ATP preparation. Author: Nagata Y, Flavin M. Journal: Biochim Biophys Acta; 1978 Mar 14; 523(1):228-35. PubMed ID: 147108. Abstract: Preparations of ATP from equine muscle contained an inhibitor of dynein Mg2+-activated ATPase. The inhibitory material was separated from the ATP by molecular sieve filtration. The several molecular species of dynein extracted from three different axonemal sources were all inhibited; myosin ATPase was not. With increasing amounts of inhibitor the inhibition did not go to completion but reached a plateau when the rate had been reduced to 1/5 the uninhibited rate. A plot of 1/[S] against 1/v at several inhibitor concentrations yielded parallel lines. There was little inhibition of dynein ATPase when Mg2+ was replaced by Ca2+. The inhibitor appeared slightly smaller in molecular size than ATP, had anionic character, and was not adsorbed to charcoal.[Abstract] [Full Text] [Related] [New Search]