UNSTEADY RATE OF ATP HYDROLYSIS BY MYOSIN AND ACTOMYOSIN IN ITS INITIAL PHASE
نویسندگان
چکیده
منابع مشابه
Regulation of actin-activated ATP hydrolysis by arterial myosin.
Myosin was isolated from the main pulmonary artery of swine and was phosphorylated or dephosphorylated by utilizing the endogenous kinase or phosphatase, respectively. The myosins, phosphorylated to various degrees, were purified free of kinase and phosphatase activities by gel filtration on Sepharose CL-4B agarose columns. The level of actin-activated ATPase activity was dependent upon the deg...
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The conditions for optimal rates of ATP hydrolysis catalyzed by the chloroplast ATP-synthase (A TPase), CFoF,, after isolation and reconstitution into asolectin liposomes have been investi gated. The rate of ATP hydrolysis was measured either after oxidation of CF0F, (by incubation with iodosobenzoate) or after reduction of CFoF, (by incubation with dithiothreitol). In both cases a rate of abo...
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The hydrolysis of ATP by acto-HMM has been studied during the transient state using a rapid-mixing apparatus. The rate of substrate binding was slightly slower and the rate of hydrolysis of the first molecule of ATP was essentially the same as for heavy meromyosin (HMM) alone. The rate of acto-HMM dissociation after binding substrate was too fast to measure in a stopped-flow apparatus, conseque...
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The kinetics of binding and hydrolysis of ATP by bovine cardiac myosin subfragment 1 has been reinvestigated. More than 90% of the total fluorescence amplitude associated with ATP hydrolysis occurs with an apparent second-order rate constant of 8.1 X 10(5) M-1 S-1 and a limiting rate constant of approximately 140 S-1 (100 mM KCl, 50 mM 1,3-bis-[tris(hydroxymethyl)methylamino]-propane, 10 mM MgC...
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ژورنال
عنوان ژورنال: The Japanese Journal of Physiology
سال: 1958
ISSN: 1881-1396,0021-521X
DOI: 10.2170/jjphysiol.8.95