Wu Di, Minton Allen P
Section on Physical Biochemistry, Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, U.S. Department of Health and Human Services , Bethesda, Maryland 20892, United States.
J Phys Chem B. 2015 Feb 5;119(5):1891-8. doi: 10.1021/jp510918d. Epub 2015 Jan 26.
The dependence of static light scattering upon the compositions of solutions including hen egg white ovalbumin, hen egg white ovomucoid, ribonuclease A, and binary mixtures of these proteins at total concentrations of up to about 40 g/L were measured at different values of the pH and ionic strength. At the pH values of measurement, ovalbumin and ovomucoid have a net negative charge and ribonuclease A has a net positive charge. The observed dependence of scattering intensity upon solution composition may be accounted for by an extension of previously formulated equivalent hard particle models that allows for the presence of both repulsive interactions between like species and attractive interactions between unlike species in mixtures of positively and negatively charged proteins.
在不同的pH值和离子强度下，测量了静态光散射对溶液组成的依赖性，这些溶液包括鸡蛋清卵清蛋白、鸡蛋清卵类粘蛋白、核糖核酸酶A以及这些蛋白质的二元混合物，总浓度高达约40 g/L。在测量的pH值下，卵清蛋白和卵类粘蛋白带净负电荷，核糖核酸酶A带净正电荷。观察到的散射强度对溶液组成的依赖性，可以通过扩展先前制定的等效硬粒子模型来解释，该模型考虑了带正电和带负电蛋白质混合物中同类物种之间的排斥相互作用以及不同类物种之间的吸引相互作用。
