PMID: 2115452Jun 1, 1990Paper

NADPH-dependent reductases of the dog lens

Experimental Eye Research
S Sato, P F Kador

Abstract

The presence of several NADPH-dependent reductases has been observed in the dog lens. Applying the purification procedures of gel filtration, affinity chromatography and chromatofocusing to dog lens homogenates resulted in the purification of aldose reductase. This enzyme appeared similar to dog kidney aldose reductase in molecular weight, isoelectric point, kinetic properties, and susceptibility to inhibition by aldose reductase inhibitors. Evidence for the presence of trace amounts of aldehyde reductase in the dog lens was also observed, although this enzyme is not present in sufficient quantities for isolation and characterization. The presence of a labile third enzyme that is immunologically distinct from either aldose reductase or aldehyde reductase was also detected. This enzyme utilizes only glyceraldehyde as substrate and is not inhibited by aldose reductase inhibitors.

References

Jul 1, 1988·Medicinal Research Reviews·P F Kador
Jun 1, 1981·Analytical Biochemistry·P F KadorJ H Kinoshita

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Citations

Nov 1, 1996·Journal of Diabetes and Its Complications·S FukaseP F Kador
Mar 1, 1996·The International Journal of Biochemistry & Cell Biology·M A SchaffhauserP F Kador
Mar 8, 2007·Journal of Ocular Pharmacology and Therapeutics : the Official Journal of the Association for Ocular Pharmacology and Therapeutics·Peter F KadorMilton Wyman
Oct 20, 2000·American Journal of Veterinary Research·D SalgadoB M Spiess
Nov 14, 2002·American Journal of Veterinary Research·Marianne RichterBernhard Spiess
Oct 28, 2009·IUBMB Life·Kent LaiKlaas J Wierenga
Jul 1, 1993·Journal of Diabetes and Its Complications·S Sato, P F Kador
Jun 18, 1999·Current Eye Research·E F SecchiP F Kador

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