Interphotoreceptor retinoid-binding protein and alpha-tocopherol preserve the isomeric and oxidation state of retinol

Photochem Photobiol. 1992 Aug;56(2):251-5. doi: 10.1111/j.1751-1097.1992.tb02154.x.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Cattle
  • In Vitro Techniques
  • Isomerism
  • Oxidation-Reduction
  • Photochemistry
  • Retinol-Binding Proteins / pharmacology
  • Rod Cell Outer Segment / metabolism*
  • Vitamin A / chemistry
  • Vitamin A / metabolism*
  • Vitamin E / pharmacology

Substances

  • Retinol-Binding Proteins
  • Vitamin A
  • Vitamin E