ABSTRACT
This chapter deals with the gel filtration behavior of a number of protein polypeptide chains in various kinds of denaturants such as SDS, urea, and guanidine hydrochloride and describes the electrostatic interaction between the gel surfaces and protein polypeptide chains. The effects of SDS concentration on the exclusion patterns and the positions of peaks were investigated in the concentration range 0.05—1% SDS. The amount of SDS-binding to the polypeptides is saturated at the cm.c. because only SDS molecules dispersed take part in the binding. As the cm.c. depends on the salt concentration of buffer solution, special attention should be paid to the experimental conditions in SDS system. The plot of some polypeptide-SDS complexes which had highly negative charges also substantially followed the common curve. The repulsive interaction between negatively charged polypeptide-SDS complexes and gel surfaces may be taken as negligibly small in the selected condition of buffer solution.
