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Journal of Dairy Science Vol. 51 No. 11 1849-
© 1968 by American Dairy Science Association ®
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Simultaneous Phenotyping Procedure for Milk Proteins—Improved Resolution of the ß-Lactoglobulins

R. Aschaffenburg1 and W. Michalak2

National Institute for Research in Dairying Shinfield, Reading, England

ABSTRACT

The procedure of starch gel electrophoresis for the simultaneous phenotyping of the principal proteins of cow's milk described by Aschaffenburg and Thymann (1) suffers from the drawback that the ß-lactoglobulin bands are not so well separated from the leading ß-casein band as to permit recognition of the rare, slow-moving ß-lactoglobulin Variant C. Nor has it been possible to resolve the recently discovered Variant D (2) which migrates even slower. One of us (3) has published an improved method which provides clear resolution of these slow-moving ß-lactoglobulins. Michalak's (3) gels were longer than, and twice as thick (3 mm) as those used by Aschaffenburg and Thymann. Attempts to adapt his method to gels of the dimensions recommended by these authors met with an unexpected diffculty. Though improved resolution was obtained, the gels were disfigured by an irregular band (salt boundary?) forming across the region of the {kappa}-caseins. The difficulty was overcome by changing the buffer systems, eliminating the borate ion which appeared to be implicated, and the following modifications are recommended when it is desired to use gels of the original dimensions.

FOOTNOTES

1 Present address: Laboratory of Molecular Biophysics, University of Oxford, England.

2 Present address: Polish Academy of Sciences, Department of Animal Experimental Breeding, Warsaw, Poland.






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Copyright © 1968 by the American Dairy Science Association ®.