Electrophoresis of Milk Proteins. I. Some Comparisons of Salt-Acid and Salt-Lyophilized Whey Fractions,

Abstract

Electrophoretic studies were made of whey proteins prepd. at pH 7.6 by 2 procedures, namely salt-acid and salt-lyophilized. Electrophoretic patterns of whey proteins prepd. by either method contained 6 electrophoretically distinguishable peaks indicating no qualitative difference in the nature of the 2 whey protein prepns. There were, however, quantitative differences. The electrophoretic concn. of euglobulin by the salt-acid method was less than half the salt-lyophilized value, while for the pseudoglobulin the salt-acid value was nearly double that of the salt-lyophilized. This change of concn. could have been due to action of the acid upon the immune lacto-globulins. Electrophoretic investigation of the non-protein filtrate from the salt-acid method of prepn. seemed to confirm this belief. In general relative percentages of component areas from salt lyophilized whey proteins were in closer agreement with the work of other investigators than those obtained by the salt-acid method.