The cephalopod retina contains two photopigments that are spatially separated within the photoreceptors; rhodopsin, localized in the light-sensitive rhabdoms, and retinochrome, present in the myeloid bodies of the photoreceptor inner segments. In the light, the chromophore of retinochrome, all-trans retinal, is photoisomerized to 11-cis to form metaretinochrome. Metaretinochrome is believed to serve as a store for 11-cis retinal used in the regeneration or biosynthesis of rhodopsin. Previous studies suggest that a soluble retinal binding protein (RALBP) serves as a shuttle between retinochrome and rhodopsin, and, in the dark, may transport chromophore from the myeloid bodies to the rhabdoms. Our study supports this hypothesis and demonstrates that RALBP is in the correct cellular locations to function as a shuttle. Dark- and light-adapted octopus retinas were labeled with anti-RALBP using immunofluorescence and immunogold techniques. Our results showed that RALBP was distributed differently in the dark- and light-adapted retinas. Our most significant observation was that myeloid bodies from light-adapted retinas were more heavily labeled by anti-RALBP than myeloid bodies in dark-adapted retinas. The rhabdomeres, interphotoreceptor matrix, and inner limiting membrane were also labeled in both light and dark conditions. Based on these results and evidence from previous biochemical studies, we conclude that in the dark RALBP leaves the myeloid bodies and transports 11-cis retinal to the rhabdoms where chromophore exchange with metarhodopsin may occur.