Isolation and characterization of rat liver aldehyde reductase.
A systematic investigation of potential ligands for the affinity purification of aldehyde reductase (alcohol:NADP+ oxidoreductase, EC 1.1.1.2.) has been carried out. The most suitable nucleotide ligands tested were NADP+ and 2',5'-ADP. Adsorbed enzyme could be eluted with NADPH but not NADH. The chlorotriazinyl dyes Cibacron Blue F3GA and Procion Red HE3B also proved effective as 'affinity' ligands when immobilized to Sepharose 4B. The free dyes and also Blue Dextran (Cibacron Blue F3GA coupled to dextran) were all potent inhibitors of aldehyde reductase. The inhibition by Blue Dextran was shown to be competitive with respect to NADPH (Ki = 1.8 x 10(-7) M). The enzyme was sensitive to inhibition by glutaric acid derivatives, flavonoids and a range of anti-convulsants.
D000244:Adenosine Diphosphate / Q000494:pharmacology; D000445:Aldehyde Oxidoreductases / Q000037:antagonists & inhibitors / Q000302:isolation & purification*; D000818:Animals; D002846:Chromatography, Affinity; D008099:Liver / Q000201:enzymology*; D008297:Male; D009249:NADP / Q000494:pharmacology; D051381:Rats; D013347:Subcellular Fractions / Q000201:enzymology
D009249:NADP; D000244:Adenosine Diphosphate; D000445:Aldehyde Oxidoreductases