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Updated: Apr 18, 2026
Characterization of Proteins by Size-Exclusion Chromatography Coupled to Multi-Angle Light Scattering SEC-MALS
Published on: June 20, 2019
Quantitative characterization of nonspecific self- and hetero-interactions of proteins in nonideal solutions via
1Section 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.
Abstract:
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.
