High-Speed Gel Filtration of Polypeptides in Sodium Dodecyl Sulfate

Abstract

The separation of polypeptides treated with SDS was studied using G3000SW packing prepared from silica for high-speed gel filtration. The peaks of ovalbumin, chymotrypsinogen A, cytochrome c, aprotinin, and insulin B chain were completely separated in the presence of 0.1% SDS and 0.05 NI sodium phosphate buffer (pH 7.0). A plot of the logarithm of molecular weight of polypeptides versus K_d was linear over a molecular weight range of 3, 000 to 50, 000 at the above concentrations of SDS and sodium phosphate. The slopes of the plots of log molecular weight versus K_d depend to a significant extent on the concentration of the sodium phosphate buffer (pH 7.0).