Yoshimura T, Matsushima A, Aki K
Biochim Biophys Acta. 1979 Dec 14;581(2):316-24. doi: 10.1016/0005-2795(79)90251-4.
Candida krusei cytochrome c forms a molecular complex with phosphorprotein phosvitin in weakly alkaline solution of low ionic strength. At most, about 22 molecules of cytochrome c bind to a phosvitin molecule. The complex at the binding ratio below about 11 (half of the maximum ratio) as a much higher binding strength. Several lines of evidence indicate that the marked difference in the binding strength is due to the difference in negative charges on phosvitin molecule concerned in the binding of a cytochrome c molecule. The phosvitin-bound cytochrome c seems to have a preferred orientation with the front surface of the molecule containing the exposed heme edge in contact with the phosvitin molecule.
克鲁斯假丝酵母细胞色素c在低离子强度的弱碱性溶液中与磷蛋白卵黄高磷蛋白形成分子复合物。最多约22个细胞色素c分子与一个卵黄高磷蛋白分子结合。结合比低于约11（最大结合比的一半）时的复合物具有高得多的结合强度。几条证据表明，结合强度的显著差异是由于参与细胞色素c分子结合的卵黄高磷蛋白分子上负电荷的差异。与卵黄高磷蛋白结合的细胞色素c似乎具有一种优先取向，即分子中含有暴露血红素边缘的前表面与卵黄高磷蛋白分子接触。
