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Departments of Dairy, Chemistry and Agricultural Chemistry Michigan Agricultural Experiment Station, East Lansing
ABSTRACT
Electrophoretic analyses of the minor-protein fraction in various buffers and at various hydrogen-ion concentrations indicate that this fraction is composed of at least two components or complexes.
Best electrophoretic resolution and enantiographic patterns of all of the whey proteins were effected with veronal-citrate buffer at a pH of 7.6.
Electrophoretic patterns obtained with whey and heat-coagulated-whey serum proteins indicate that the heat labile whey components were effectively removed by the fractionation procedure employed in this work.
1 Published with the approval of the Director of the Michigan Agricultural Experiment Station as Journal Article no. 1227.
2 This article is part of a dissertation presented to the Faculty of the Graduate School of Michigan State College in partial fulfillment of the requirements for the degree of Doctor of Philosophy.
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