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Apparent Immunological Similarity of Bovine ß-lactoglobulins A, B, and C

Department of Dairy Science University of Illinois, Urbana

ABSTRACT

In the development of a quantitative immunological procedure designed after the procedures of Oudin to determine the ß-lactoglobulin content of milk and other materials (7), it was found that rabbit antisera prepared to a mixture of ß-lactoglobulin A and B reacted equally well with either the pure A or B form and thus these two proteins appeared to be immunologically indistinguishable, (rough and Jenness (4) and DeWeer et al. (3), using specific antisera prepared against both the A and the B forms in various procedures including the double diffusion Ouchterlony plate tests and immunoelectropho-resis, also indicated the similar immunological identity of the two proteins.

Subsequently, Bell (1) discovered a third genetic polymorph of this protein now called ß-lactoglobulin C. Bell and McKenzie (2) concluded from various qualitative immunological analyses that the C form also appeared to be immunologically the same as the A and B forms. However, it has been shown that rabbit antisera prepared to bovine ß-lactoglobulins A and B also reacts with the ß-lactoglobulins isolated from goat and sheep milk (5) and that goat ß-lactoglobulin could not be distinguished from bovine ß-lactoglobulin by precipitin tests or by the Ouchterlony method (8).