Human aldehyde dehydrogenase. Activity with aldehyde metabolites of monoamines, diamines, and polyamines
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چکیده
منابع مشابه
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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Aldehyde dehydrogenases (ALDH) are a family of enzymes that efficiently detoxify aldehydic products generated by reactive oxygen species and might therefore participate in cell survival. Because ALDH activity has been used to identify normal and malignant cells with stem cell properties, we asked whether human myogenic precursor cells (myoblasts) could be identified and isolated based on their ...
متن کاملHorse 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 ...
متن کاملAldehyde dehydrogenase. Covalent intermediate in aldehyde dehydrogenation and ester hydrolysis.
4-trans-(NN-Dimethylamino)cinnamaldehyde (an aldehyde, DACA) and 4-trans-(NN-dimethylamino)cinnamoylimidazole (an amide, DACI) have been shown to be substrates for human aldehyde dehydrogenase (EC 1.2.1.3) which form chromophoric covalent intermediates. The spectra of covalent intermediates from both the cytoplasmic (E1) and mitochondrial (E2) isoenzymes derived from DACA and DACI were compared...
متن کاملYeast Aldehyde Dehydrogenase
The potassium-activated, pyridine nucleotide-linked aldehyde dehydrogenase from yeast has been purified to the stage of homogeneity as judged by ultracentrifugation and gel electrophoresis. The enzyme has been crystallized, although this is not a recommended step in purification because loss of catalytic activity is thereby incurred. At least three separable, active fractions were obtained with...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1991
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)98796-x