Horse Liver Aldehyde Dehydrogenase

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Horse Liver Aldehyde Dehydrogenase

Horse liver aldehyde: NAD oxidoreductase (EC 1.2.1.3) has been purified to homogeneity by a procedure consisting of salt fractionation, ion exchange chromatography, and isoelectric focusing. The purif?ed material has a turnover number of 1.85 pmoles of NADH per min per mg of protein when assayed at pH 9.0 with propionaldehyde as substrate. Values obtained for the molecular weight of the native ...

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Horse liver aldehyde dehydrogenase. I. Purification and characterization.

Horse liver aldehyde: NAD oxidoreductase (EC 1.2.1.3) has been purified to homogeneity by a procedure consisting of salt fractionation, ion exchange chromatography, and isoelectric focusing. The purif?ed material has a turnover number of 1.85 pmoles of NADH per min per mg of protein when assayed at pH 9.0 with propionaldehyde as substrate. Values obtained for the molecular weight of the native ...

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Horse liver aldehyde dehydrogenase. Purification and characterization of two isozymes.

Two isozymes of horse liver aldehyde dehydrogenase (aldehyde, NAD oxidoreductase (EC 1.2.1.3)), F1 and F2, have been purified to homogeneity using salt fractionation followed by ion exchange and gel filtration chromatography. The specific activities of the two isozymes in a pH 9.0 system with propionaldehyde as substrate were approximately 0.35 and 1.0 mumol of NADH/min/mg of protein for the F1...

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Human Liver Aldehyde Dehydrogenase

Human liver aldehyde dehydrogenase has been found to be capable of hydrolyzing p-nitrophenyl esters. Esterase and dehydrogenase activities exhibited identical ion exchange and affinity properties, indicating that the same protein catalyzes both reactions. Competitive inhibition of esterase activity by glyceraldehyde and chloral hydrate furnished evidence that p-nitrophenyl acetate was hydrolyze...

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Rate-limiting steps for the esterase and dehydrogenase reaction catalyzed by horse liver aldehyde dehydrogenase.

Horse liver aldehyde dehydrogenase, like other aldehyde dehydrogenases, is capable of hydrolyzing esters such as nitrophenyl acetate. Pre-steady state and burst kinetics were performed using substrate levels of enzyme to determine whether the rate-limiting step occurred prior to or after the formation of an acyl enzyme intermediate. A burst was found by both techniques for the dehydrogenase rea...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1972

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(19)45784-0