Purification and characterization of four NADPH-dependent aldehyde reductases from pig brain.
By a procedure involving ammonium sulfate precipitation, gel filtration, and affinity chromatography, four aldehyde reductases (ALRs) were purified to enzymatic homogeneity from pig brain. These enzymes, designated ALR1, ALR2, ALR3, and succinic semialdehyde reductase were chemically and physically identical with, respectively, the high-Km aldehyde reductase, the low-Km aldehyde reductase, carbonyl reductase, and succinic semialdehyde reductase of other tissues and species. The purification procedure allows the purification of these enzymes from the same tissue homogenate in amounts sufficient for characterization and other enzymatic studies. This methodology should be applicable to the simultaneous and rapid purification of aldehyde reductases from other tissues.
D000429:Alcohol Oxidoreductases / Q000302:isolation & purification*; D000818:Animals; D001921:Brain / Q000201:enzymology*; D002458:Cell Fractionation; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D013237:Stereoisomerism; D013379:Substrate Specificity; D013552:Swine; D005680:gamma-Aminobutyric Acid / Q000031:analogs & derivatives / Q000302:isolation & purification
D005680:gamma-Aminobutyric Acid; D000429:Alcohol Oxidoreductases; C019642:alcohol dehydrogenase (NADP+); C009338:succinic semialdehyde