Retinol-binding proteins in bovine interphotoreceptor matrix
Biochemical and Biophysical Research CommunicationsPublished 1 October 1982
Alice J. Adler, Katherine J. Martin
Citations142
SJR quartileQ2
SJR score0.75
SNIP0.56
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TL;DR
Interphotoreceptor matrix material from bovine eyes contains 1.8 nmoles per eye of vitamin A in light- Adapted eyes and 0.7 in dark-adapted eyes, nearly all as unesterified retinol, which constitutes a significant fraction of theitamin A in the retina-IPM-retinal pigment epithelium functional complex.
Abstract
Interphotoreceptor matrix (IPM) material from bovine eyes contains 1.8 nmoles per eye of vitamin A in light-adapted eyes and 0.7 in dark-adapted eyes, nearly all as unesterified retinol. This constitutes a significant fraction of the vitamin A in the retina-IPM-retinal pigment epithelium functional complex. Two distinct, non-serum retinol-carrying proteins are abundant in the IPM. One of these, of MW 17000, may be the cellular retinol-binding protein present in retina and pigment epithelium. Even more retinol is bound, in the light-adapted IPM, to a protein of MW ∼ 290,000; this binding is greatly reduced in the dark. These retinol-binding proteins may function in transporting vitamin A through the IPM for the visual cycle.
Keywords
Materials ScienceBiochemistry, Genetics and Molecular Biology
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