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ARS, USDA, Eastern Regional Research Center, Philadelphia, PA 19118
ABSTRACT
ß2-Microglobulin has been isolated from several species, but only bovine ß2-microglobulin, previously known as lactollin, has been crystallized. An improved method for its isolation from colostrum is described. The bovine homologue exhibits a concentration-dependent aggregation behavior. ß2-Microglobulin is related to both immune and histocompatibility antigen systems. It exhibits homology with the constant domains of the immunoglobulin-G light and heavy chains and is an integral part of histocompatibility antigens bound to cell surface. ß2-Microglobulin also occurs in the free state in various body fluids including milk and colostrum. The possible relationship of elevated free ß2-microglobulin to pathological conditions is suggested for future research.
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