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ABSTRACT
The
-casein component of the casein system of milk, which appears as a single, leading electrophoretic peak at pH 8.6, is heterogeneous and should he referred to as the
-casein fraction. The components comprising this fraction vary in distribution, dependent upon the experimental conditions. Alpha-casein has been separated into calcium-sensitive and calcium-insensitive fractions which have been designated by various symbols. These fractions usually are in the form of an
(Ca sensitive)—
(Ca insensitive) complex in equilibrium with its components. In view of the complexity of the
-casein fraction, this Committee feels that no recommendations on nomenclature should be made at this time. Cherbuliez's
-casein, Hammersten's proteose, and the 2% and 12% TCA-soluble peptides of Alais and Nitschmann, materials apparently derived from
-casein by various procedures, are discussed in this report.
ß-lactoglobulin, obtained from mixed milk, is composed of at least two forms of ß-lactoglobulin which are genetically determined and referred to as ß-lactoglobulins A and B, discernible by paper electrophoresis in veronal buffer at pH 8.6, where Type A constitutes the leading component. Further, Type A associates in acetate buffer between pH 3.7 and 5.2 and is essentially monomeric at pH values alkaline to its isoelectric point, whereas Type B exists in its monomeric form under similar conditions. These characteristics explain in part the electrophoretic and ultracentrifugal heterogeneity of normal (mixed) ß-lactoglobulins A + B and ß-lactoglobulin A.
1 Department of Dairy, Michigan State University, East Lansing.
2 Department of Dairy-Food Industries, University of Wisconsin, Madison.
3 Research and Development Div., National Dairy Products Corporation, Oakdale, Long Island.
4 Department of Dairy Science, University of Illinois, Urbana.
5 Department of Food Technology, University of Illinois, Urbana.
6 Eastern Utilization Research Branch, USDA, Philadelphia, Pa.
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