Reaction intermediates of H-meromyosin-ATPase and ultraviolet difference spectrum of H-meromyosin induced by ATP.
UV Difference spectra of H-meromyosin (HMM) during the steady state of the myosin-ATPase reaction [EC 3.6.1.3] were measured in 1.5 and 0.05M KC1 in the presence of 5mM MgC1(2) and 20mM Tris-HC1 at pH 8.0 and 24 degrees, using pyruvate kinase [EC 2.7.1.40] and phosphoenolpyruvate to regenerate ATP. It was found that the difference spectrum and its dependence on ATP concentration were the same in 1.5M KC1 as in 0.05M KC1. On the bases of these and other results, the nature of the intermediates of HMM ATPase in the steady-state reaction of HMM ATPase was discussed.
D000251:Adenosine Triphosphatases / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000494:pharmacology*; D000818:Animals; D015879:Myosin Subfragments / Q000378:metabolism*; D009218:Myosins / Q000378:metabolism; D011189:Potassium Chloride / Q000494:pharmacology; D011817:Rabbits; D013056:Spectrophotometry, Ultraviolet
D015879:Myosin Subfragments; D011189:Potassium Chloride; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases; D009218:Myosins