It has been hypothesized that interphotoreceptor retinoid‐binding protein (IRBP) functions as a two‐way carrier of retinoid between the retinal pigment epithelium (RPE) and rod photoreceptors in the vertebrate eye. This hypothesis has been tested in recent studies that have employed purified, initially ligand‐free, bovine IRBP and the “RPE‐eyecup” obtained from the toad (Bufo marinus) eye. The present experiments further characterize the IRBP/RPE‐eyecup system with respect to (i) the solubilization and protection of retinol by IRBP, and (ii) the time course of IRBP‐mediated release of 11‐cis retinal by the RPE. The data, together with previous findings in the IRBP/RPE‐eyecup preparation, support the view that 11‐cis retinal is the principal retinoid released by the RPE into IRBP‐supplemented aqueous medium, and that IRBP in vivo promotes the regeneration of rhodopsin by facilitating the exchange of retinoid between bleached rods and the RPE.