Purification and properties of an NADPH-linked aldehyde reductase from rat kidney.
Rat kidney was shown to contain two NADPH-linked aldehyde reductases (alcohol:NADP+) oxidoreductase, EC 1.1.1.2) with different substrate affinities. The high-Km aldehyde reductase, which was purified to apparent homogeneity, had a molecular weight of 32 000 as determined by Sephadex G-100 gel filtration, and of 37 000 by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. The purified enzyme reduced various aliphatic aldehydes of different carbon-chain lengths besides many chemicals containing aldehyde groups. The Km values for n-hexadecanal and n-octadecanal were 8 microM and 4 microM, respectively. Bovine serum albumin (1.8 mM) stimulated the reduction of n-hexadecanal and n-octadecanal, and increased the Vmax values by about 15-fold without changing the Km values. The kidney enzyme was not distinguishable from the brain and liver high-Km aldehyde reductases in mobility on polyacrylamide gel electrophoresis, immunological properties, peptide maps or substrate specificity.
D000429:Alcohol Oxidoreductases / Q000302:isolation & purification* / Q000378:metabolism; D000818:Animals; D001921:Brain / Q000201:enzymology; D002918:Chymotrypsin / Q000378:metabolism; D005779:Immunodiffusion; D007668:Kidney / Q000201:enzymology*; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D008970:Molecular Weight; D051381:Rats; D012710:Serum Albumin, Bovine / Q000378:metabolism; D013379:Substrate Specificity
D012710:Serum Albumin, Bovine; D000429:Alcohol Oxidoreductases; C019642:alcohol dehydrogenase (NADP+); D002918:Chymotrypsin