The photopigments, rhodopsin and retinochrome, have been localized in cephalopod retinae using light and electron microscopic immunocytochemical methods. Polyclonal antibodies prepared against squid opsin demonstrated the presence of this protein in the photoreceptor rhabdomes, Golgi zone, Golgi-associated vesicles, plasma membrane, large cytoplasmic vesicles, and axonal membranes of octopus retinae. Monoclonal anti-opsin immunostained the rhabdomes and multivesicular bodies in the photoreceptor inner segments of squid. We believe the multivesicular bodies are involved in rhabdome turnover. Polyclonal anti-retinochrome localized this photopigment to the myeloid bodies of the photoreceptor inner segments, the rhabdomes, and to the extracellular space between opposing rhabdomeres in octopus retina. The results suggest some interesting functional relationships between rhodopsin and retinochrome with regard to chromophore exchange between illuminated forms of these photopigments and chromophore addition to newly synthesized opsin.