Abstract
IT has been shown that papain-solubilised HL-A antigens consist of two polypeptide chains, which may be separated under dissociating conditions1,2. Peterson et al.3 have shown that β-2-microglobulin (β-2-m) constitutes one of the two polypeptide chains in papain-solubilised HL-A antigens. In these antigens, β-2-m represents a constant small subunit (molecular weight 11,800), whereas a larger subunit (30,000–31,000) carries the allo-antigenic specificity. The studies by Peterson et al. do not exclude the possibility that the two subunit structure of HL-A antigens might be a product of the solubilisation process. It has previously been reported4 that β-2-m, which also occurs in biological fluids5, is present in high concentrations on the surface of lymphocytes. The present study was designed to establish whether β-2-m is part of the intact HL-A molecule in the cell membrane. Experiments were performed in which the blocking of HL-A antigens6,7, β-2-m and other lymphocyte membrane components were induced by selected ahtisera. Furthermore, to study the relationship between these cell membrane components and the antigen receptors on lymphocytes, the different antisera were also tested for their ability to induce or inhibit lymphocyte activation in vitro. Methodological details are published elsewhere8.
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SOLHEIM, B., THORSBY, E. β-2-Microglobulin is part of the HL-A molecule in the lymphocyte membrane. Nature 249, 36–38 (1974). https://doi.org/10.1038/249036a0
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DOI: https://doi.org/10.1038/249036a0
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