Conversion of a NADPH-dependent aldehyde reducing enzyme into aldose reductase.
1. Aldose reductase, aldehyde reductase and high-Km aldose reductase were purified from the inner medulla of dog kidney. 2. Compared with aldose reductase, high-Km aldose reductase had a lower isoelectric point, a lower activity for aldo-sugars and a lower sensitivity for aldose reductase inhibitors, and it was not activated by sulfate ions. Both reductases had the same molecular weight (38,500) and immunochemical properties. 3. High-Km aldose reductase was easily converted into an aldose reductase-like enzyme, namely a generated reductase upon incubation in neutral buffer solution. 4. The generated reductase was identical with aldose reductase with respect to the isoelectric point, substrate specificity, activation by sulfate ions and IC50 values for aldose reductase inhibitors. The generated reductase revealed immunochemical identity with aldose reductase as well as high-Km aldose reductase.
Ohta
M
M
Division of Biological Chemistry and Biologicals, National Institute of Hygienic Sciences, Tokyo, Japan.
Tanimoto
T
T
Tanaka
A
A
Hayakawa
T
T
D000449:Aldehyde Reductase / Q000737:chemistry*; D000818:Animals; D004285:Dogs; D007120:Immunochemistry; D007679:Kidney Medulla / Q000201:enzymology*; D007700:Kinetics; D009249:NADP / Q000502:physiology*; D013379:Substrate Specificity
D009249:NADP; D000449:Aldehyde Reductase