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Electrophoresis of Milk Proteins II. Some Effects of Methods of Preparation on the Electrophoretic Patterns of Whey Proteins¹

Department of Chemistry, Kansas State College, Manhattan

ABSTRACT

Conclusions: The composition of the protein components evidently was modified by at least three of the four methods used in preparing whey proteins for electrophoresis. The difference in peak areas at pH 5.8 is one evidence of such modification. Differences in the mobilities and isoelectric points of corresponding components are other evidences. The increased number and mobility of peaks in the "non-protein" filtrate also indicate modification of the original components.

Isoelectric points for the albumin and ß-lactoglobulin fractions from all four preparations (pH 4.8) were lower than literature values (pH 5.2) for electrophoresis of purified components. However, they were all higher than the value (pH 4.5) from viscosity studies of milk. Probably, then, the nature of all components reflected changes induced by all four methods used in their preparation.

¹ Contribution no. 422. Department of Chemistry, Kansas State College, Manhattan. Presented before the Agriculture and Food Section of the American Chemical Society in Chicago, September, 1950.

² Contains portions of a thesis to be presented by W. G. Stanley as partial fulfillment of the requirements for the degree Doctor of Philosophy in Chemistry at Kansas State College.