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On the Heterogeneity of ß-Lactoglobulin¹

Department of Dairy Technology and Institute of Nutrition and Food Technology, The Ohio State University, Columbus

ABSTRACT

ß-Lactoglobulin, the principal milk serum protein, has been the subject of much investigation (6) since it was first obtained in a crystalline form by Palmer (5). It has been well characterized with respect to electrophoretic mobility, sedimentation constant, and molecular weight (2).

Since 1955, when Aschaffenburg (1) reported the occurrence of two electrophoretically different forms (A and B) of ß-lactoglobulin, research has been concerned to a large measure in studying differences in their electrophoretic, sedimentation, and light-scattering properties, to demonstrate the mechanism for molecular interactions among their monomeric forms (7–10). For example, it was shown that an association of ß-lactoglobulin molecules occurs between pH 3.5 and 5.2 to form tetramers and other aggregates (9), and that its heterogeneity at pH values close to the isoelectric point (pH 4.79–6.04) is due to the presence of both A and B forms of ß-lactoglobulin (7).

In the present study, additional evidence was gained concerning the heterogeneity of ß-lactoglobulin by the use of polyacrylamide-gel disc electrophoresis and Sephadex gel-filtration.

¹ Article No. 3-64, Department of Dairy Technology. Supported by a grant from the National Institutes of Health.