Goding J W, Walker I D
Proc Natl Acad Sci U S A. 1980 Dec;77(12):7395-9. doi: 10.1073/pnas.77.12.7395.
Spleen cells from BALB/c and C57BL/6 mice were cultured separately or together, and the biosynthetically labeled supernates were examined by two-dimensional polyacrylamide gel electrophoresis. Although there were no major labeled proteins in the mixed group that were not present in the separate cultures, there was a major low-molecular-weight protein that differed in charge in the two strains. This protein was identified as beta 2-microglobulin; it could be labeled with 125I on the cell surface by using the lactoperoxidase technique, was noncovalently attached to the H-2K molecule, and had the expected size and charge when compared with human beta 2-microglobulin. Both acidic and basic forms were present in (BALB/c X C57BL/6) F1 hybrids, suggesting codominant expression, although allelic exclusion was not ruled out. Either parental form could combine with one parental form of the H-2K molecule. The beta 2-microglobulin gene does not appear to be closely linked to either the H-2 or th immunoglobulin heavy-chain complexes. It is proposed that beta 2-microglobulin is an "effector subunit" of histocompatibility antigens and that its physiological role is to interact with a specific killing structure on the surface of cytolytic T lymphocytes and thereby initiate cell destruction.
将BALB/c和C57BL/6小鼠的脾细胞分别或共同培养,并用二维聚丙烯酰胺凝胶电泳检测生物合成标记的上清液。尽管混合组中不存在单独培养时未出现的主要标记蛋白,但有一种主要的低分子量蛋白在两个品系中的电荷不同。这种蛋白被鉴定为β2-微球蛋白;通过乳过氧化物酶技术可在细胞表面用125I进行标记,与H-2K分子非共价结合,与人类β2-微球蛋白相比具有预期的大小和电荷。酸性和碱性形式在(BALB/c×C57BL/6)F1杂种中均存在,提示共显性表达,尽管不排除等位基因排斥。任一亲本形式都可与H-2K分子的一种亲本形式结合。β2-微球蛋白基因似乎与H-2或免疫球蛋白重链复合体均无紧密连锁。有人提出β2-微球蛋白是组织相容性抗原的“效应亚基”,其生理作用是与溶细胞性T淋巴细胞表面的特定杀伤结构相互作用,从而启动细胞破坏。