Abstract
β2-Microglobulin (β2-m) is a highly conserved polypeptide (12,000 molecular weight; 12K) noncovalently associated with the heavy chain (45–48K) of the major histocompatibility complex (MHC) class I antigens. Its synthesis is required for expression of the HLA-A/B and H–2K/D heavy chains at the cell surface1; β2-m is also associated with the human cell-surface antigens T6 and M241 isolated from thymocytes2–6. However, on the T leukaemic cell line MOLT-4 some of the T6 antigens contain a different 12K subunit, termed βt (refs 3, 7, 8). Purified human β2-m can exchange partially both with human β2-m associated with HLA-antigens9, and with mouse β2-m associated with murine alloantigens10, 11. As MOLT-4 cells were grown in the presence of fetal calf serum (FCS) and as serum is known to contain some free β2-m12, we examined whether βt was bovine β2-m which had replaced endogenous β2-m on the surface of the cell. Here we show both that β2-m from FCS or human serum (HuS) used in cell culture can exchange with β2-m on the cell surface, and that βt is in fact bovine β2-m.
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Bernabeu, C., van de Rijn, M., Lerch, P. et al. β2-Microglobulin from serum associates with MHC class I antigens on the surface of cultured cells. Nature 308, 642–645 (1984). https://doi.org/10.1038/308642a0
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DOI: https://doi.org/10.1038/308642a0
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