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Journal of Dairy Science Vol. 71 No. 5 1141-1146
© 1988 by American Dairy Science Association ®
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The Method of Aschaffenburg and Drewry for the Crystallization of ß-Lactoglobulin and {alpha}-Lactalbumin. 1. Electrophoresis of Fractions and the Calcium2+/Ethylenebis (Oxyethylenenitrilo) Tetraacetic Acid Shift of {alpha}-Lactalbumin

Marvin P. Thompson and Dorothy P. Brower

United States Department of Agriculture, Agricultural Research Service, Eastern Regional Research Center, 600 E. Mermaid Lane, Philadelphia, PA 19118

ABSTRACT

ß-Lactoglobulin and {alpha}-Lactalbumin were isolated and crystallized by the classical method of Aschaffenburg and Drewry, and the purity of the crystals was assessed by native PAGE and SDS-PAGE. Although ß-lactoglobulin was free of contaminants, {alpha}-lactalbumin was still contaminated after five recrystallization steps. Yields of crystals in this study were lower than reported by Aschaffenburg and Drewry. Further, it was observed that {alpha}-lactalbumin undergoes a Ca2+/Ca2+ free, dependent electrophoretic shift characteristic of many calcium-binding proteins.






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Copyright © 1988 by the American Dairy Science Association ®.