| Literature DB >> 4129801 |
P A Peterson, L Rask, J B Lindblom.
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.Entities:
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Year: 1974 PMID: 4129801 PMCID: PMC387926 DOI: 10.1073/pnas.71.1.35
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN: 0027-8424 Impact factor: 11.205