Abstract

Abstract The maximum amount of sodium dodecyl sulfate (SDS) bound to a number of proteins in the presence of high SDS concentrations (1 to 2 g/100 ml) was determined and found to vary between 1.1 and 2.2 g of SDS per g of protein. The charge of the protein caused a variation in amount bound by 20 to 50%, while raising the ionic strength from 0.1 to 0.4 increased the binding by 35 to 100%. Glucose oxidase did not bind or lose activity in 1 g of SDS per 100 ml. Papain and pepsin were much more resistant to binding and activity loss than other proteins. All other single chained proteins bound SDS within 3 hours. Most proteins composed of subunits bound SDS much more slowly, invariably dissociating to the subunit.

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