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

DOI:
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发表时间:
1974
影响因子:
4
通讯作者:
B. Solheim
B. Solheim
中科院分区:
医学2区
文献类型:
--
作者:
B. Solheim

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最近的数据表明,被木瓜蛋白酶或温和去污剂溶解的HL-A抗原由两条多肽链组成,这两条多肽链可以在解离条件下分离(Creswell等人1973,Tanigaki等人1973,Springer &,Strominger 1973)。木瓜蛋白酶处理细胞膜并分离HL-A抗原后,得到分子量约为31,000和11,000的多肽链;而通过去污剂溶解的HL-A抗原具有分子量约为43,000和11,000的多肽。在血浆和尿液中也发现了较小的碎片(Miyakawa 等人,1973)。彼得森等人。 (1972)报道了β2-微球蛋白(β-2-m),其是存在于人类生物体液中的低分子量蛋白质(11,600)(Berggard &. Beam 1968),以高浓度存在于白细胞表面。最近,几个小组(Grey等人,1973年,Nakamuro等人,1973年,Peterson等人,1974年)已经证明,π-2-m似乎与用非离子去污剂或木瓜蛋白酶处理淋巴细胞膜制备的HL-A分子中发现的小共同亚基相同。然而,不能排除HL-A的两个亚基结构可能是增溶过程的产物。
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.