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Molecular weight distributions of proteins by equilibrium ultracentrifugation and gel filtration chromatography

University of British Columbia

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.

Text

2010-01-28

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http://hdl.handle.net/2429/19265

Food Science

University of British Columbia

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