Kinetic studies of liver alcohol dehydrogenase
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چکیده
منابع مشابه
Kinetic studies of liver alcohol dehydrogenase.
1. NADH2 prepared by enzymic reduction of pure NAD by the method of Rafter & Colowick (1957), and isolated as the sodium salt, gives higher maxrimum rates of reduction of acetaldehyde with liver alcohol dehydrogenase at pH 6 than a number of commercial preparations of high purity. Maximum values of 2-4 for the extinction ratio E260/E340 and 2% for the proportion of inactive material absorbing a...
متن کاملKinetic and mechanistic studies of methylated liver alcohol dehydrogenase.
Reductive methylation of lysine residues activates liver alcohol dehydrogenase in the oxidation of primary alcohols, but decreases the activity of the enzyme towards secondary alcohols. The modification also desensitizes the dehydrogenase to substrate inhibition at high alcohol concentrations. Steady-state kinetic studies of methylated liver alcohol dehydrogenase over a wide range of alcohol co...
متن کاملKinetic studies of dogfish liver glutamate dehydrogenase.
Initial-rate studies were made of the oxidation of L-glutamate by NAD+ and NADP+ catalysed by highly purified preparations of dogfish liver glutamate dehydrogenase. With NAD+ as coenzyme the kinetics show the same features of coenzyme activation as seen with the bovine liver enzyme [Engel & Dalziel (1969) Biochem. J. 115, 621--631]. With NADP+ as coenzyme, initial rates are much slower than wit...
متن کاملKinetic Studies of Liver Alcohol Dehydrogenase and pH with Coenzyme Preparations of High Purity Effects
Liver alcohol dehydrogenase has been the subject of repeated and detailed kinetic study. Because of its abundance, ready crystallization (1,2) and stability, the availability of pure, stable substrates, and the marked changes of absorption and fluorescence spectrum which accompany its combination with the reduced coenzyme (3), it has been to a considerable extent the immediate stimulus for the ...
متن کاملKinetic and modelling studies of NAD+ and poly(ethylene glycol)-bound NAD+ in horse liver alcohol dehydrogenase.
Poly(ethylene glycol)-bound nicotinamide adenine dinucleotide (PEG-NAD+) has been successfully employed in the continuous production of L-amino acids from the corresponding alpha-keto acids by stereospecific reductive amination. Like many other dehydrogenases also horse liver alcohol dehydrogenase (HLADH) appears to be active with PEG-NAD+ as coenzyme, although the turnover number is three to f...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1962
ISSN: 0006-2936
DOI: 10.1042/bj0840244