The interaction of a nonionic detergent with protein: I. Physical properties of the protein detergent complex

Abstract

The addition of Triton X-100, a nonionic detergent, to solutions of bovine plasma albumin resulted in a small but significant increase in intrinsic viscosity and a decrease in electrophoretic mobility. The specific optical rotation of bovine plasma albumin, ribonuclease, and oxidized ribonuclease was unchanged by the addition of detergent. The number of reactive sulfhydryl groups of bovine serum albumin and muscle aldolase was unchanged in the presence of detergent. These data indicate that no gross structural change occurs in the protein but are consistent with the view that the degree of hydration is increased in the presence of detergent.