Abstract
Publisher Summary Interstitial or interphotoreceptor retinol-binding protein (IRBP) is a large, elongated glycoprotein that is synthesized and secreted by the photoreceptor cells. IRBP is found in the interphotoreceptor matrix of the eye, where its major function is believed to be the transport of 11-cis- and all-trans-retinoids between the neural retina and retinal pigment epithelium. This chapter discusses the purification, characterization, molecular cloning, and sequence of IRBP. The first human IRBP clone (H.4 IRBP) was obtained by screening a human retina λgtl0 cDNA library with a 258-base-pair bovine probe (B23) obtained from a bovine retina λgt11 expression library. H.4 IRBP was then employed as a probe to enable isolation and purification of three overlapping human cDNA clones (H8, H12, and H18) from the same human retina λgtl0 cDNA library. Because human eyes are not available in large quantities, most biochemical studies have been carried out on the bovine protein.
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