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. 1983 Aug 1;213(2):547–550. doi: 10.1042/bj2130547

Purification and partial characterization of a rat retina alcohol dehydrogenase active with ethanol and retinol.

P Julià, J Farrés, X Parés
PMCID: PMC1152161  PMID: 6351845

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.

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Selected References

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