Published in

Portland Press, Biochemical Journal, 2(213), p. 547-550, 1983

DOI: 10.1042/bj2130547

Links

Tools

Export citation

Search in Google Scholar

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

Journal article published in 1983 by P. Julià, J. Farrés ORCID, X. Parés
This paper is available in a repository.
This paper is available in a repository.

Full text: Download

Red circle
Preprint: archiving forbidden
Orange circle
Postprint: archiving restricted
Upload
Red circle
Published version: archiving forbidden
Policy details
Data provided by SHERPA/RoMEO

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.