Coelomoic fluid protein (CP), a vitellogenin contained in the coelomic fluid of polychaetes, is transported by receptor-mediated endocvtosis that is controlled by GTP-binding proteins. Transport of 125l-CP was markedly inhibited by AlF4 and toxins such as cholera toxin and pertussis toxin. These effects appear to be mediated by cAMP, since 125l-CP transport was also greatly inhibited by dibutyryl cAMP. The results strongly suggest that hetero trimeric G-protein is involved in the regulation of 125l=CP transport through the activation of adenylyl cyclase. Immunoblotting tests with antibodies against Gsa and Gia subunits showed a Gsa subunit of 45 kDa in the membrane of oocytes of intermediate and large size classes and a Gia subunit of 41 kDa only in the oocytes of the intermediate size class.