title: Purification and partial characterization of a rat retina alcohol dehydrogenase active with ethanol and retinol.
abstract: Homogeneous alcohol dehydrogenase (ADH) from rat retina was obtained by chromatography on DEAE-Sepharose and AMP-hexane-Sepharose. The enzyme is a dimer of Mr congruent to 80000 and oxidizes ethanol using NAD+ as a cofactor. Careful activity determinations demonstrate unambiguously that rat retina ADH is active with retinol as a substrate. This result opens the question about the role of retina ADH in the visual cycle.
mesh_terms: D000426:Alcohol Dehydrogenase; D000429:Alcohol Oxidoreductases / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D000431:Ethanol / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D012160:Retina / Q000201:enzymology*; D013347:Subcellular Fractions / Q000201:enzymology; D014801:Vitamin A / Q000378:metabolism*
chemical_list: D014801:Vitamin A; D000431:Ethanol; D000429:Alcohol Oxidoreductases; D000426:Alcohol Dehydrogenase