Results 161 to 170 of about 30,602 (201)
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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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Aldose and aldehyde reductase in animal tissues
Metabolism, 1986The aldehyde reductases comprise a group of monomeric NADPH-dependent oxidoreductases with a broad and similar substrate specificity. Three major reductases, ALR1, ALR2, and ALR3, occur in tissues. The predominant one, ALR1, is aldehyde reductase; ALR2 is aldose reductase, an enzyme implicated in the etiology of diabetic complications; and ALR3 is ...
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Inhibition of Aldehyde Reductase by Carboxylic Acids
1990Aldehyde reductase (EC 1.1.1.2) and aldose reductase (EC 1.1.1.21) are structurally related, monomeric oxidoreductases that catalyze the NADPH-dependent reduction of a variety of aliphatic, aromatic and sugar aldehydes. For most substrates Km values of aldose reductase are one to two orders of magnitude lower than those of aldehyde reductase ...
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2002
This is a meeting abstract discussing aflatoxin aldehyde reductases. It comes from the meeting of the American-Chemical-Society Division of Chemical Toxicology.
Hayes, J.D. +3 more
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This is a meeting abstract discussing aflatoxin aldehyde reductases. It comes from the meeting of the American-Chemical-Society Division of Chemical Toxicology.
Hayes, J.D. +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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The structure and functions of aldehyde reductases
1981Although aldehyde reductases are widely distributed among tissues and species (Davidson et al., 1978), most interest has focussed on the mammalian brain enzymes because of their potential involvement in the metabolism of monoamine-derived aldehydes (Tipton et al., 1977).
Anthony J Turner, Susan R Whittle
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Functions of aldehyde reductases
Biochemical Society Transactions, 1981A J, Turner, S R, Whittle
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Reactivity of Enzyme Modification Reagents with Aldose Reductase and Aldehyde Reductase
1990Aldose reductase (EC 1.1.1.21) and aldehyde reductase (EC 1.1.1.2) are members of a broad family of NADPH-dependent reductases (Feldstead and Bachur, 1980). While the physiological role of either enzyme remains unknown, it is generally assumed that aldose reductase reduces aldose sugars to their respective sugar alcohols while aldehyde reductase ...
T, Mizoguchi, H, Itabe, P F, Kador
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