sorbinil and erythrose

sorbinil has been researched along with erythrose* in 1 studies

Other Studies

1 other study(ies) available for sorbinil and erythrose

Article	Year
Studies on L-threose as substrate for aldose reductase: a possible role in preventing protein glycation. Molecular and cellular biochemistry, 1996, Jun-21, Volume: 159, Issue:2 L-threose is a product of ascorbate oxidation and degradation. By virtue of its free aldehyde group it can form Schiff-bases with tissue proteins, altering their normal function. In this study, we have examined the possibility of its detoxification to L-threitol by aldose reductase in the lens. The rat lens enzyme present in fresh homogenate as well as after 100 fold purification was found to utilize L-threose with a km of 7.1 x 10(-4) M. The specificity of the reaction was affirmed by its inhibition with sorbinil and quercetin, the well known aldose reductase inhibitors. Further studies on the role of this enzyme in preventing toxicity due to degradation products of ascorbate are in progress. Topics: Aldehyde Reductase; Animals; Ascorbic Acid; Crystallins; Enzyme Inhibitors; Glycosylation; Imidazoles; Imidazolidines; Kinetics; Lens, Crystalline; NADP; Oxidation-Reduction; Quercetin; Rats; Substrate Specificity; Tetroses	1996

Article

Year

Studies on L-threose as substrate for aldose reductase: a possible role in preventing protein glycation.

Molecular and cellular biochemistry, 1996, Jun-21, Volume: 159, Issue:2

L-threose is a product of ascorbate oxidation and degradation. By virtue of its free aldehyde group it can form Schiff-bases with tissue proteins, altering their normal function. In this study, we have examined the possibility of its detoxification to L-threitol by aldose reductase in the lens. The rat lens enzyme present in fresh homogenate as well as after 100 fold purification was found to utilize L-threose with a km of 7.1 x 10(-4) M. The specificity of the reaction was affirmed by its inhibition with sorbinil and quercetin, the well known aldose reductase inhibitors. Further studies on the role of this enzyme in preventing toxicity due to degradation products of ascorbate are in progress.

Topics: Aldehyde Reductase; Animals; Ascorbic Acid; Crystallins; Enzyme Inhibitors; Glycosylation; Imidazoles; Imidazolidines; Kinetics; Lens, Crystalline; NADP; Oxidation-Reduction; Quercetin; Rats; Substrate Specificity; Tetroses

1996