Conversion of a NADPH-dependent aldehyde reducing enzyme into aldose reductase |
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| Institution: | 1. Guangzhou Key Laboratory of Subtropical Biodiversity and Biomonitoring, School of Life Sciences, South China Normal University, Guangzhou 510631, PR China;2. Guangdong Laboratory for Lingnan Modern Agriculture, Guangzhou 510642, PR China;3. Guangdong Provincial Engineering Technology Research Center for Environmentally-Friendly Aquaculture, Institute of Modern Aquaculture Science and Engineering, School of Life Sciences, South China Normal University, Guangzhou 510631, PR China |
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| Abstract: | - 1.1. Aldose reductase, aldehyde reductase and high-Km, aldose reductase were purified from the inner medulla of dog kidney.
- 2.2. 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.
- 3.3. High-Km aldose reductase was easily converted into an aldose reductase-like enzyme, namely a generated reductase upon incubation in neutral buffer solution.
- 4.4. 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.
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