Titlebook: Alcohol and Aldehyde Metabolizing Systems-IV; Ronald G. Thurman Book 1980 The Editor(s) (if applicable) and The Author(s), under exclusive

搖曳

廣口瓶

松馳

Carbon-13 Magnetic Resonance Probe of Coenzyme and Inhibitor Binding in Liver Alcohol Dehydrogenaseion binding site at the zinc of the carboxymethylated enzyme may require re-evaluation. The electron density at the zinc of the modified enzyme may be better explained as being due to unsuspected binding of imidazole.

Fantasy

Multifunctionality of Liver Alcohol Dehydrogenasees. However, their binding/catalytic domains may be nonequivalent albeit overlapping. This is deduced from the following observations: (a) chain length specificities for homologous substrates, (b) cross effects of analogous substrates or products and (c) different responses to various chemical modifications.

Antecedent

pancreas

Genetic Regulation of Alcohol Dehydrogenase, Aldehyde Dehydrogenase and Aldehyde Oxidase Isozymes inale reproductive tissues. Ahd-1 (encoding AHD-A.) was found on chromosome 4 near Gpd-1 (encoding the liver isozyme of glucose-6-phosphate dehydrogenase), whereas the aldehyde oxidase loci (Aox-1, Aox-2) were closely linked on chromosome 1 near Id-1 (encoding isocitrate dehydrogenase).

Torrid

動作謎

On the Possible Relationship of Cytochrome P-450 to Alcohol Metabolism: Fundamental Aspects of the M, and substrate (benzphetamine) facilitates the binding of reductase. The possible effect of ethanol on these interactions should be considered in evaluating the reported inhibition by high concentrations of ethanol of reactions catalyzed by liver microsomal cytochrome P-450.

忘川河

Evolution of Aldehyde Reductase: An Immunological Approach to the Relatedness of Aldehyde Reductase ed from compositional comparisons. A UEP of 12 is approximately half that of lactate dehydrogenase and shows that aldehyde reductase is evolving at twice the rate of glycolytic enzymes. This may indicate a relatively non-essential metabolic role for the enzyme.

討厭

Properties of Adlehyde Dehydrogenase from Chemically-Induced Rat Hepatomas and Normal Rat Liveromposed (50%) of a hepatoma-specific isozyme (IV), differing in several properties from isozymes I–III; the remainder of the tumor cytosolic activity is due to isozyme III (48%). The data indicate that expression of the tumor-specific aldehyde dehydrogenase phenotype requires both qualitative and qu