Purification and characterization of oocyte vitellin from Perinereis cultrifera (polychaete annelid).
Vitellin was identified and purified from submature oocytes of Perinereis cultrifera by concanavalin-A - Sepharose 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% 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.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D004527:Egg Proteins / Q000276:immunology / Q000302:isolation & purification*; D005260:Female; D006023:Glycoproteins / Q000032:analysis; D046911:Macromolecular Substances; D008970:Molecular Weight; D009865:Oocytes / Q000032:analysis*; D011077:Polychaeta / Q000032:analysis*
D000596:Amino Acids; D004527:Egg Proteins; D006023:Glycoproteins; D046911:Macromolecular Substances