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Procedure for Simultaneous Phenotyping of ß-Casein and ß-Lactoglobulin Variants in Cow's Milk

Dairy Science Department, Utah State University, Logan

ABSTRACT

Aschaffenburg and Thymann (2), using thin starch gels in an alkaline medium, obtained simultaneous patterns for ß-casein and ß-lactoglobulin, as well as the other principal proteins of cow's milk. Later, however, it was shown by Peterson and Kopfler (3) that ß-casein A could be separated into three distinct components by vertical polyacrylamide gel electrophoresis in acid media. This necessitates a second gel run to obtain the correct ß-casein phenotype. Aschaffenburg (1) showed that this could be accomplished using horizontal thin starch gel electrophoresis. This technique, however, failed to resolve any of the other milk proteins.

Using slight modifications of Aschaffenburg's (1) technique, the ß-lactoglobulins may be very clearly resolved. They migrate a considerable distance (approximately 5 cm) ahead of the ß-caseins, thus overcoming the major objection of close proximity of these in alkaline media.

The following procedure was used in obtaining the results shown in Fig. 1.