Abstract
A MEMBRANE fragment of human lymphoid cells obtained by papain digestion has been found to be composed of two subunits which differ in molecular weight1,2. The heavy molecular weight subunit (33,000 daltons) carries the HL-A serologically defined (SD) antigens while the light molecular weight subunit (11,000 daltons) carries antigenic determinents reacting with antiserum directed against β2 microglobulin (β2m)3–6. Treatment of human lymphocytes with antisera directed against the HL-A SD antigens results in capping of these antigens7; addition of β2m antibody to lymphocytes will likewise cause capping of the HL-A SD antigens8,9. Furthermore, activation of lymphocytes in mixed leukocyte culture (MLC) can be inhibited by β2m antibody9,10. These data suggested to the investigators9,10 that the HL-A subunit and/or the β2m subunit may be part of the same receptor complex of the T lymphocyte. This concept is supported by the recent studies of β2m demonstrating extensive homology between β2m and the constant regions of the heavy chain (and the light chain) of immunoglobulin IgG111,12. Consequently β2m was thought to have a recognition function similar to that of immunoglobulin.
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