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. 1974 Jan;71(1):35-9.
doi: 10.1073/pnas.71.1.35.

Highly purified papain-solubilized HL-A antigens contain beta2-microglobulin

P A Peterson, L Rask, J B Lindblom

Highly purified papain-solubilized HL-A antigens contain beta2-microglobulin

P A Peterson et al. Proc Natl Acad Sci U S A. 1974 Jan.

Abstract

HL-A antigens comprising 11 different antigenic specificities were isolated after papain solubilization of spleen-cell membrane constituents. During the entire purification procedure, beta(2)-microglobulin appeared together with the HL-A antigens. The highly purified antigens were composed of two polypeptide chains. The large subunit carried the antigenic specificity whereas the small polypeptide chain was very similar, if not identical, to beta(2)-microglobulin. The two HL-A antigen polypeptide chains were held together by noncovalent interactions only, and beta(2)-microglobulin, isolated from urine, could replace the small subunit in forming a complex with the large polypeptide chain. The topographical relationship in the cell membrane between beta(2)-microglobulin and the large HL-A antigen polypeptide chain is unknown. The two polypeptide chains may be fortuitously bound as a result of the solubilization procedure.

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