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• W2000353675 abstract "Starch-gel electrophoresis of rat ocular tissues shows two anodic isoenzymes of alcohol dehydrogenase (ADH), designated as ADH-1 and ADH-2. ADH-1 is characteristic of the ocular tissues, and corresponds to more than 95% of all ADH activity in the eye. The well known cathodic forms of rat liver ADH, that we named ADH-3, are not observed in the ocular tissues. ADH-1 is detected in retina, pigment epithelium-choroid, ocular fluid, and cornea but not in the lens. The cornea exhibits the highest ADH activity [200±59 milliunits (munits) mg−1] followed by the pigment epithelium-choroid (11±7 munits mg−1). Activity in the retina is very small (0·6±0·2 munit mg−1) and represents only 0·6% of the total activity in the eye. Most of the rat ocular ADH is localized in the cornea (68%) where it could play a significant role in the detoxication of the alcohols of a broad range of structures. Purified ADH-1 shows a low Km for retinol oxidation (20 μm) and for retinal reduction (30 μm) indicating that this isoenzyme may have a function in the metabolism of retinoids. Ethanol competitively inhibits retinol oxidation, but with a very high apparent inhibition constant (0·6 m) demonstrating that the inhibitory effect is not significant at the usual concentrations found in the blood during ethanol intoxication." @default.
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• W2000353675 date "1986-04-01" @default.
• W2000353675 modified "2023-10-17" @default.
• W2000353675 title "Ocular alcohol dehydrogenase in the rat: Regional distribution and kinetics of the ADH-1 isoenzyme with retinol and retinal" @default.
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• W2000353675 doi "https://doi.org/10.1016/0014-4835(86)90023-0" @default.
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