Abstract
Retinol dehydrogenase activity in subcellular fractions obtained from bovine pigment epithelium was attributable to two particulate oxidoreductases. One of these enzymes, all- trans retinol dehydrogenase, was present in the rod outer segment discs undergoing digestion in the phagolysosomes, and probably does not normally interconvert retinal and retinol in the pigment epithelium. The other enzyme, 11- cis retinol dehydrogenase, was present in the light membrane fractions, and probably functions (by its retinaldehyde reductase activity) to return the chromophore of rhodopsin, 11- cis retinal, to the ocular pool of vitamin A compounds.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
