National Center for Macromolecular Hydrodynamics, School of Biosciences, University of Nottingham, Sutton Bonington LE12 5RD, United Kingdom.
J Phys Chem B. 2011 Sep 15;115(36):10725-9. doi: 10.1021/jp2006149. Epub 2011 Aug 22.
Examination of the solution behavior of ovalbumin by small-angle X-ray scattering, dynamic light scattering, and analytical ultracentrifugation methods confirms its existence as a 44-kDa monomer in 20 mM phosphate, pH 7.0, thereby contradicting the discord introduced by published SAXS studies in favor of a dimeric state for this protein at neutral pH. Although the theoretical interpretation of SAXS measurements considers the consequences of thermodynamic nonideality arising from the repulsive interactions between molecules only if they give rise to a positive second virial coefficient, the fact that A(2) is negative for the present system does not account for the earlier findings.
通过小角 X 射线散射、动态光散射和分析超速离心等方法研究卵清蛋白的溶液行为，证实其在 20mM 磷酸盐（pH7.0）中以 44kDa 的单体形式存在，这与发表的 SAXS 研究结果相矛盾，后者支持该蛋白在中性 pH 下呈二聚体状态。尽管 SAXS 测量的理论解释仅考虑了分子间排斥相互作用引起的热力学非理想性的后果，如果它们导致正的第二维里系数，但对于本系统，A(2)为负，这并不能解释早期的发现。
