Interaction of sodium dodecyl sulphate with a soluble keratin

Abstract

Electrophoretic studies have shown that sodium dodecyl sulphate combines with α-keratose in solution in amount far in excess of that required for stoichiometric binding to the positive groups on the protein. However, an amount equivalent to the number of positive sites on the protein is more firmly bound than the remainder. The variation of the relative viscosity and sedimentation coefficients with the amount of sodium dodecyl sulphate present on the protein has been attributed to changes in the configuration and state of aggregation of the protein molecules. A molecular weight of approximately 48,000 has been determined for a-keratose in the presence of sodium dodecyl sulphate.