Vitellin was identified and purified from submature oocytes of Perinereis cultrfera by concanavalin-ASepharose and Ultrogel AcA 34 column chromatography. The yolk protein was defined as a glycolipoprotein with a relative molecular mass of' 380000. Upon dissociation by sodium dodecyl sulphate, vitellin was shown to release five polypeptide subunits which ranged in relative molecular mass from 98000 -16000. The purified vitellin was further characterized by amino acid analysis and its lipid and carbohydrate contents. The molecule contained about 5 % carbohydrate and 16'x lipid. Antiserum prepared against vitellin was shown to react with a component from the coelomic fluid of maturing females. Thus, it was suggested that in nereid annelids, considered phylogenetically and morphologically primitive, oocyte differentiation might depend upon the incorporation of a vitellogenin as in insects and many oviparous vertebrates.The sexuality of Nereids (Polychaeta worms) has been extensively studied. Many authors have demonstrated the existence of a brain neurohormone which inhibits oogenesis and somatic transformations of the epitoky [l -31. Studying the endocrinal determination of oogenesis, Durchon and Porchet [4] found a correlation between the brain hormonal production and the oocyte metabolism. During the juvenile phase characterized by an important production of brain hormone, yolk granules appear in the oocytic ooplasm (vitellogenesis) whereas at the time of genital submaturity, in absence of brain hormone, the oocytes produce cortical alveoli.While hormonal determination of oogenesis and cytology of the oocytes have been the object of several biological investigations [4 -81, relatively few biochemical studies have been carried out on the oocyte metabolism among the Nereidae. Concerning vitellogenesis, yolk synthesis has been shown to occur within the oocyte from small molecular weight precursors such as amino acids and monosaccharides (process termed autosynthesis) in Nel-eis divcwicolor, Perinereis cultr(fet,9, 101. However, Fischer [Ill, using Nereis virens, demonstrated the presence of a vitellin-like antigen in the coelomic fluid of mature females suggesting the heterosynthetic origin of the yolk. In Perinereis cultrifkra, immunological studies by Dhainaut et al. [I21 revealed identical antigens in the oocytes and coelomic fluid of females, but no significant evidence of an involvement of this material in yolk synthesis was obtained.Among annelids, reports on yolk protein remain limited to N . virens vitellin [13]. This protein, isolated by a method including DEAE-cellulose and phosphocellulose chromatography, has been characterized as a lipoglycoprotein of apparent Mr of 420000 and from its amino acid composition, appears to resemble insect vitellins. Apart from these gross features, Nereis vitellin remains poorly characterized. With interest in the hormonal control of vitellin synthesis as well as in its evolutionary relationship among annelids and other invertebrates, further studies of vitellins are requi...