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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1974 Jan;71(1):35–39. doi: 10.1073/pnas.71.1.35

Highly Purified Papain-Solubilized HL-A Antigens Contain β2-Microglobulin

Per A Peterson 1, Lars Rask 1, J Bertil Lindblom 1
PMCID: PMC387926  PMID: 4129801

Abstract

HL-A antigens comprising 11 different antigenic specificities were isolated after papain solubilization of spleen-cell membrane constituents. During the entire purification procedure, β2-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 β2-microglobulin. The two HL-A antigen polypeptide chains were held together by noncovalent interactions only, and β2-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 β2-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.

Keywords: polypeptide chains, spleen-cell membranes, histocompatibility determinants

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Selected References

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