Purification and immunolocalization of a vitellin-like protein from the Pacific oyster Crassostrea gigas

A female-specific protein from the hemolymph, and a related ovarian protein were identified in the Pacific oyster Crassostrea gigas using immunological procedures. The latter protein was isolated from ovarian extract by a combination of precipitation in distilled water, ammonium sulfate fractionation, hydroxylapatite chromatography and gel filtration on a Sepharose 6B column, and was identified as a macromolecular glycolipoprotein of ∼500 kD; sodium dodecylsulfate polyacrylamide gel electrophoresis, under reducing conditions, revealed seven heterogeneous polypeptides. Using a specific antiserum against purified protein, we also examined the immunohistochemical distribution of the protein at light- and electron-microscopic levels. Light microscopy revealed its presence in the oocytes, and electron microscopy identified it in yolk granules and the vitelline coat of the oocytes. These results indicate that the purified protein is a vitellin-like protein. Since no organ other than the ovary reacted with the antiserum, it is probable that the protein is produced inside the ovary, probably autosynthetically by oocytes.