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Changes in Whey Proteins between Drying and Colostrum Formation

Department of Clinical Pathology

F. A. Murphy² and Ole Aalund³

Department of Veterinary Microbiology, University of California, Davis

ABSTRACT

In a previous report (3) it was shown by paper electrophoresis that a whey protein (designated X) migrating between -lactalbumin and the immune globulin fraction appeared in very high concentration following a short period of agalactia due to experimental mastitis. A similar protein has also been demonstrated in whey obtained from a dry cow 45 days prepartum by Larson (6) and at 27 days prepartum by McMeekin (7), using free-boundary electrophoresis. However, paper electrophoresis of dry-cow whey protein fractions separated by DEAE cellulose using step-wise NaCl gradients for elution never revealed a protein with the paper electrophoretic mobility of the X protein (2). Those fractions designated immune globulin were characterized solely by their paper electrophoretic behavior and by the similar elution pattern exhibited by immune globulin fractions salted out of whey by classical techniques. Electrophoretically, these proteins migrated within the -globulin zone of blood serum or the immune globulin zone of whey.

² Present address: Virology Section, Communicable Disease Center, Atlanta, Georgia.

³ Present address: Department of Hygiene and Bacteriology, Royal Veterinary and Agricultural College, Copenhagen, Denmark.