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This report describes methods and results obtained by combining the techniques of sodium dodecyl sulfate (SDS) gel electrophoresis and electrophoresis in discontinuous buffer systems. The SDS gel system utilizes a sulfate-borate discontinuity which stacks and unstacks protein-SDS complexes over a range of 2,300 to 320,000 daltons, providing high resolution fractionation. The properties of protein-SDS complexes are investigated by calculating retardation coefficients and apparent free mobilities from Ferguson plots. Apparent free mobilities are approximately constant, establishing a linear relationship between the logarithm of the relative mobility and the retardation coefficient. The retardation coefficient is shown both empirically and theoretically to be a uniform function of molecular weight of protein-SDS complexes over specified ranges, providing a rationale for determining molecular weight from plots of the negative logarithm of relative mobility against molecular weight.
David M. Neville (Fri,) studied this question.