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Molecular weight distributions of proteins by equilibrium ultracentrifugation and gel filtration chromatography Ma, Ching-Yung

Abstract

The molecular weight distributions (MWDs) of some proteins were determined by equilibrium ultracentrifugation and gel filtration chromatography (GPC). A linear programming technique was used to compute MWDs from equilibrium data. The light-scattering second virial coefficient (BLS) of one protein, ovalbumin, was determined and was used to correct for the non-ideal behavior of the polymers. For unimodal systems, good MWDs were obtained from single experiment without correction for non-ideality. For more complex systems, combination of data from several experiments performed at different rotor speeds was required to give reasonable distributions; and correction for BLS brought about further improvement in the smoothness and accuracy of the MWDs. GFC was found to be a rapid and convenient method for MWD determination, having better resolving power than the linear programming technique. The advantages and limitations of these two methods were discussed.

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