The Mechanism of Triosephosphate Dehydrogenase Inactivation by Reduced Diphosphopyridine Nucleotide
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چکیده
منابع مشابه
The mechanism of triosephosphate dehydrogenase inactivation by reduced diphosphopyridine nucleotide.
We have shown in a previous communication (1) that the enzyme triosephosphate dehydrogenase is rapidly inactivated in the presence of reduced diphosphopyridine nucleotide at physiological concentrations, temperature, and pH. Good stoichiometry was shown for the amount of enzyme inactivation, DPNH-X1 formation, and disappearance of sulfhydryl groups. It was then of particular interest to determi...
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From the particulate reduced nicotinamide adenine dinucleotide (DPNH) oxidase of beef heart, Mackler (3) has obtained a soluble DPNH dehydrogenase which was estimated to be approximately 90 to 95% homogenous when examined electrophoretically.l Similarly, when the enzyme was chromatographed on diethylaminoethyl cellulose with phosphate buffer, pH 7.5, in a gradient elution method (0.001 M to 0.0...
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In continuation of our investigation of liver diphosphopyridine nucleotide-linked aldehyde dehydrogenase (1)) we have undertaken a study of various classes of inhibitors of the enzyme. Interest in aldehyde oxidation has been increasing in recent years from several points of view. The classical problem of ethanol oxidation in viva still has many unresolved facets (Z), and the enzymes responsible...
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DPNH-X was prepared as described previously (1) ; the barium salt was converted to the sodium salt before use, and solutions were stored at 20”. Concentrations of DPNH-X were calculated with an extinction coefficient of 13.5 X lo6 sq. cm. mole-’ at 290 rnM (1). Sodium salts of ADP, ATP, ITP, UTP, and crystalline disodium ATP were obtained from the Pabst Laboratories, Milwaukee, Wisconsin. Myoki...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1962
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)50152-6