受体介导的卵黄蛋白原与鸡卵母细胞的结合
Receptor-mediated vitellogenin binding to chicken oocytes.
作者信息
Yusko S, Roth T F, Smith T
出版信息
Biochem J. 1981 Oct 15;200(1):43-50. doi: 10.1042/bj2000043.
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).
对卵黄蛋白原与鸡卵母细胞膜的特异性结合进行了表征。这种主要的母鸡血清磷脂糖蛋白及其一种低分子量成分——卵黄高磷蛋白，以约6×10⁻⁷ M的解离常数（KD值）与卵母细胞膜结合。结合的最适pH为6.0，与卵黄内容物的pH相同。卵黄高磷蛋白和卵黄蛋白原相互竞争结合；所测试的其他蛋白质竞争程度不同。按重量计含10%磷酸盐的卵黄高磷蛋白似乎是受体识别的多肽。RNA不能与卵黄蛋白原或卵黄高磷蛋白竞争结合，这表明结合特异性可能需要的不仅仅是聚合磷酸盐。这种结合具有组织特异性，因为卵黄高磷蛋白和卵黄蛋白原在pH 6.0和7.5时都能与卵母细胞表面结合，但在任何pH下都不与鸡红细胞结合。
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