Results 191 to 200 of about 186,754 (233)

Aldose and aldehyde reductases in human tissues

Biochimica et Biophysica Acta (BBA) - General Subjects, 1984
Immunochemical 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, N H, Ansari, G A, Hair, B, Das   +3 more
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Stereospecificity of hydrogen transfer of aldehyde reductase

Experientia, 1979
Aldehyde 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, J D, Münch, J P, von Wartburg   +2 more
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Multiple Aldehyde Reductases of Human Brain

1980
Human 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, B, Wermuth, J P, von Wartburg   +2 more
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Fatty acid reductase in bioluminescent bacteria. Resolution from aldehyde reductases and characterization of the aldehyde product

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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Aldose and aldehyde reductase in animal tissues

Metabolism, 1986
The 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

1990
Aldehyde 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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Aflatoxin aldehyde reductases

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., Kelly, V.P., Slattery, C.M., Ellis, E.M.   +3 more
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The structure and functions of aldehyde reductases

1981
Although 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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Biogenic Aldehyde Metabolism in Rat Brain: Subcellular Distribution of Aldose Reductase and Valproate‐Sensitive Aldehyde Reductase

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, S R, Whittle, J, Hryszko, S R, Guha   +3 more
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Functions of aldehyde reductases

Biochemical Society Transactions, 1981
A J, Turner, S R, Whittle
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