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- W2000595041 abstract "Lens Polyol dehydrogenase was purified approximately 1000-fold from calf lenses and the properties of the enzyme were studied. The enzyme appears to be a metallo-enzyme and is reactivated, after inhibition by EDTA, by magnesium ion. β-mETOH lowers the threshold concentration for magnesium ion. Furthermore, NADH prevents EDTA inhibition. The pH optima for the forward and reverse reactions were pH 9 and pH 7 respectively. The following Km values were determined: xylitol, 2·08 × 10−3 m; sorbitol, 1 × 10−2 m; NAD, 2·7 × 10−5 m; and, fructose, 3·2 × 10−2 m. Additionally, it was found that NADH, a product of the forward reaction, is an enzyme inhibitor. Thus, the concentration of sorbitol in the lens and the ratio of NADNADH may play important roles in regulating the activity ofolyol dehydrogenase activity in vivo as well as in vitro." @default.
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- W2000595041 date "1973-06-01" @default.
- W2000595041 modified "2023-09-23" @default.
- W2000595041 title "Lens Polyol dehydrogenase" @default.
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- W2000595041 doi "https://doi.org/10.1016/0014-4835(73)90304-7" @default.
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