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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.

SUBMITTER: Julia P 

PROVIDER: S-EPMC1152161 | biostudies-other | 1983 Aug

REPOSITORIES: biostudies-other

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