Association between the β‐2‐m/HL‐A Molecule and Membrane Structures Responsible for Lymphocyte Activation
Association between the β‐2‐m/HL‐A Molecule and Membrane Structures Responsible for Lymphocyte Activation
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β-2-m/HL-A 分子与负责淋巴细胞激活的膜结构之间的关联
作者:
B. Solheim
Recent data indicate that HL-A antigens solubilized by papain or mild detergents consist of two polypeptide chains which may be separated under dissociating conditions (Creswell et al. 1973, Tanigaki et al. 1973, Springer &, Strominger 1973). After papain treatment of cell membranes and separation of the HL-A antigens., polypeptide chains with molecular weight of about 31,000 and 11,000 are obtained; whereas the HL-A antigens solubilized by detergents have polypeptides of molecular weight of about 43,000 and 11,000. The smaller fragment has also been found in plasma and urine (Miyakawa et al. 1973). Peterson et al. (1972) have reported that /?2-microglobulin (/?-2-m), which is a low molecular weight protein (11,600) occurring in human biological fluids (Berggard &. Beam 1968), is present in high concentrations on the surface of leucocytes. Recently several groups (Grey et al. 1973, Nakamuro et al. 1973, Peterson et al. 1974) have demonstrated that /?-2-m seems to be identical to the small common sub-unit found in HL-A molecules prepared by treatment of lymphocyte membranes with non-ionic detergents or by papain. However, it could not be ruled out that the two sub-unit structure of HL-A might be a product of the solubilization process.