Evidence supporting the identity of beef heart mitochondrial chloroform-released adenosine triphosphatase (ATPase) with coupling factor I |
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Authors: | Vitaly L Spitsberg James E Blair |
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Institution: | 1. Institute for Enzyme Research, University of Wisconsin, Madison, Wisc. 53706 U.S.A.;2. Milton College, Milton, Wisc. 53563 U.S.A. |
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Abstract: | Highly purified mitochondrial chloroform-released beef heart ATPase had molecular weight 330 000, five bands (α, β, γ, δ, ε) in sodium dodecyl sulfate gel electrophoresis and could restore the oxidative-phosphorylation function of A particles. Maximal inhibition (90%) of the enzyme by N,N′-dicyclohexylcarbodiimide was achieved at a molar ratio of inhibitor to protein of 30 : 1. Chloroform introduced into an aqueous solution of beef heart coupling factor I protected it from cold inactivation. |
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Keywords: | A particles submitochondrial particles prepared by sonication of beef heart mitochondria in an ammonia solution at pH 9 2 DCCD |
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