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Multiple Aldehyde Reductases of Human Brain
1980Human brain contains four forms of aldehyde reducing enzymes. One major activity, designated AR3, has properties indicating its identity with the NADPH-dependent aldehyde reductase, EC 1.1.1.2. The other major form of human brain enzyme, AR1, which is also NADPH-dependent, reduces both aldehyde and ketone-containing substrates, including vitamin K3 ...
P L, Hoffman +2 more
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Structure and Mechanism of Aldehyde Reductase
1995Aldehyde reductase (ALR1, EC 1.1.1.2) and aldose reductase (ALR2, EC 1.1.1.21) catalyze the NADPH-dependent reduction of a wide range of aromatic and aliphatic aldehydes to their corresponding alcohols. Despite a recently expressed opinion that aldose reductase is of little consequence (Harding, 1992) the past few years have seen a great advancement in
T G, Flynn +3 more
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Aldehyde dehydrogenase and aldehyde reductase in isolated bovine brain microvessels
Alcohol, 1985The activities of aldehyde dehydrogenase and aldehyde reductase were measured in microvessel fractions isolated from bovine brain. Aldehyde dehydrogenase specific activity in microvessels was enriched 1.5-fold over that measured in grey matter. The specific activity of aldehyde reductase was significantly lower in parenchymal vessles and microvessels ...
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Stereospecificity of hydrogen transfer of aldehyde reductase
Experientia, 1979Aldehyde reductase from human liver catalyzes the hydrogen transfer from the pro-4R position on the dihydronicotinamide ring of the coenzyme to the re face of the carbonyl carbon atom of the substrate.
B, Wermuth +2 more
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Aldose and aldehyde reductases in human tissues
Biochimica et Biophysica Acta (BBA) - General Subjects, 1984Immunochemical characterizations of aldose reductase and aldehyde reductases I and II, partially purified by DEAE-cellulose (DE-52) column chromatography from human tissues, were carried out by immunotitration, using antisera raised against the homogenous preparations of human and bovine lens aldose reductase and human placenta aldehyde reductase I and
S K, Srivastava +3 more
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Journal of Neurochemistry, 1982
Abstract: Reductase activity towards two aldose substrates has been examined in subcellular fractions prepared from rat brain. The reduction of glucuronate, which is sensitive to inhibition by the anticonvulsant drug sodium valproate, corresponds to the major high‐Km aldehyde reductase in brain.
A J, Turner +3 more
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Abstract: Reductase activity towards two aldose substrates has been examined in subcellular fractions prepared from rat brain. The reduction of glucuronate, which is sensitive to inhibition by the anticonvulsant drug sodium valproate, corresponds to the major high‐Km aldehyde reductase in brain.
A J, Turner +3 more
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Physiological Relevance of Aldehyde Reductase and Aldose Reductase Gene Expression
1999Carbonyl compounds which are produced as intermediate metabolism during ordinary metabom or are present in food or drugs are known to be toxic to living organisms because of their high degree of reactivity. It has also been suggested that elevation in protein carbonyl groups is also a likely cause of aging (Stadtman, 1992).
J, Fujii +5 more
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Canadian Journal of Biochemistry, 1981
Fatty acid reductase from the bioluminescent bacterium Photobacterium phosphoreum, has been partially purified free of aldehyde reductase activity and with a low endogenous fatty acid content permitting the characterization of the aldehyde product of the reaction.
D, Riendeau, E, Meighen
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Fatty acid reductase from the bioluminescent bacterium Photobacterium phosphoreum, has been partially purified free of aldehyde reductase activity and with a low endogenous fatty acid content permitting the characterization of the aldehyde product of the reaction.
D, Riendeau, E, Meighen
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Biochemical Pharmacology, 1979
Abstract Three NADPH-linked aldehyde reductases (F1, F2 and F3) could be separated by DEAE-cellulose chromatography from rabbit liver cytosol. These enzymes could be distinguished in regard to molecular weight, mobility in polyacrylamide gel electrophoresis, pH optima, substrate specificity and inhibitor sensitivity.
H, Sawada, A, Hara
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Abstract Three NADPH-linked aldehyde reductases (F1, F2 and F3) could be separated by DEAE-cellulose chromatography from rabbit liver cytosol. These enzymes could be distinguished in regard to molecular weight, mobility in polyacrylamide gel electrophoresis, pH optima, substrate specificity and inhibitor sensitivity.
H, Sawada, A, Hara
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