The specific binding of vitellogenin to chicken oocyte membranes was characterized. This major hen serum phospholipoglycoprotein and one of its lower-molecular-weight components, phosvitin, bound to oocyte membranes with KD values of approx. 6 x 10-7 M. The optimum pH for binding was 6.0, the same as the pH of yolk contents. Phosvitin and vitellogenin compete with each other for binding; other proteins tested do not compete to the same degree. Phosvitin, which contains 10% phosphate by weight, appears to be the polypeptide recognized by the receptor. RNA failed to compete with either vitellogenin or phosvitin for binding, suggesting that the binding specificity may require more than polymeric phosphate. The binding was tissue-specific in that phosvitin and vitellogenin bound to oocyte surfaces (at both pH 6.0 and 7.5), but not to chicken erythrocytes (at either pH).
