Abstract
Vitamin K quinone was shown to be an effective inhibitor of vitamin K epoxide reduction by whole rat liver microsomes. Observation of inhibition was dependent upon the mode of addition of the substrate and inhibitor suggesting segregation of the compounds into different microsomal vesicles under certain conditions. The result is consistent with reduction of both vitamin K quinone and vitamin K epoxide by a single enzyme or a multisite enzyme complex.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Dithiothreitol / pharmacology*
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Epoxy Compounds / metabolism*
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Ethers, Cyclic / metabolism*
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Kinetics
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Microsomes, Liver / enzymology*
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Mixed Function Oxygenases / metabolism*
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NADH, NADPH Oxidoreductases / metabolism*
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Oxidation-Reduction
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Quinone Reductases / metabolism*
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Rats
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Tritium
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Vitamin K / metabolism*
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Vitamin K Epoxide Reductases
Substances
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Epoxy Compounds
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Ethers, Cyclic
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Tritium
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Vitamin K
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Mixed Function Oxygenases
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Vitamin K Epoxide Reductases
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NADH, NADPH Oxidoreductases
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Quinone Reductases
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Dithiothreitol