Interphotoreceptor retinoid-binding protein and alpha-tocopherol preserve the isomeric and oxidation state of retinol.
Retinol decomposes rapidly into a number of products, including its aldehyde form, retinal, when introduced into buffer in phospholipid vesicles or ethanol. Interphotoreceptor retinoid-binding protein at low concentrations is found to protect retinol from isomerization and oxidation. The addition of alpha-tocopherol to either liposomes or an ethanolic-buffer solution also prevents decomposition. Neither of these agents interferes with the successful regeneration of pigment with 9-cis retinal in rod outer segment preparations or the restoration of sensitivity by retinoids in isolated rod photoreceptors.
Crouch
R K
RK
Department of Ophthalmology, Medical University of South Carolina, Charleston 29425.
Hazard
E S
ES
Lind
T
T
Wiggert
B
B
Chader
G
G
Corson
D W
DW
D000818:Animals; D002417:Cattle; D066298:In Vitro Techniques; D007536:Isomerism; D010084:Oxidation-Reduction; D010777:Photochemistry; D012177:Retinol-Binding Proteins / Q000494:pharmacology; D012374:Rod Cell Outer Segment / Q000378:metabolism*; D014801:Vitamin A / Q000737:chemistry / Q000378:metabolism*; D014810:Vitamin E / Q000494:pharmacology
D012177:Retinol-Binding Proteins; D014801:Vitamin A; D014810:Vitamin E