Purification and Properties of Six Aldo-Keto Reductases from Rat Adrenal Gland

• Published in: Journal of biochemistry (Tokyo) Vol. 115; no. 5; pp. 991 - 999
• Main Authors: Inazu, Norihisa, Nagashima, Yoshio, Satoh, Tetsuo, Fujii, Tomoko
• Format: Journal Article
• Language: English
• Published: England Oxford University Press 01.05.1994
• Subjects: Adrenal Cortex - enzymology; adrenal gland; Adrenal Medulla - enzymology; Alcohol Oxidoreductases - antagonists & inhibitors; Alcohol Oxidoreductases - chemistry; Alcohol Oxidoreductases - isolation & purification; Aldehyde Reductase - antagonists & inhibitors; Aldehyde Reductase - chemistry; Aldehyde Reductase - isolation & purification; aldo-keto reductase; Aldo-Keto Reductases; Animals; carbonyl reductase; Cross Reactions; Female; Hydrogen-Ion Concentration; Immunochemistry; Isoenzymes - chemistry; Isoenzymes - isolation & purification; Male; rat; Rats; Rats, Inbred WKY; Substrate Specificity
• ISSN: 0021-924X; 1756-2651
• DOI: 10.1093/oxfordjournals.jbchem.a124450

Six aldo-keto reductases from rat adrenal gland have been highly purified to apparent homogeneity. These enzymes were identified as carbonyl reductases (CR-K1, CR-K2, CR-A, and CR-B), aldehyde reductase (AR-H), and aldose reductase (AR-L) in terms of substrate specificity, molecular weight (33,000–39,000), inhibitor susceptibility, cofactor requirement, and immunochemical properties. Both CR-K1 and CR-K2 were characterized as possessing high affinity towards 13,14-dihydro-15-ketoprostaglandin F2α and were localized immunohistochemically in the zona glomerulosa and the zona reticularis of adrenal cortex, and in the ganglion cell of adrenal medulla. Immunoreactive proteins to anti-CR-K2 antibody were observed in male and female reproductive tissues of rats. Positive immunoreactive protein to anti-CR-A antibody was found in mouse, hamster, and rabbit adrenal gland, whereas that to anti-CR-K2 antibody was present only in rat adrenal gland. AR-H and AR-L mainly reduced aromatic and aliphatic aldehydes. All the aldo-keto reductases from rat adrenal gland were completely inhibited by p-chloromercuribenzoate. Barbiturate and 3,3'-tetramethylene glutarate potently inhibited AR-H, and quercitrin significantly decreased the activity of CR-K1, CR-K2, and AR-L. We propose that these aldo-keto reductases may play important roles in the rat adrenal functions.