Cresswell P, Springer T, Strominger J L, Turner M J, Grey H M, Kubo R T
Proc Natl Acad Sci U S A. 1974 May;71(5):2123-7. doi: 10.1073/pnas.71.5.2123.
A number of immunological methods have been employed to show that the small subunit of HL-A antigens, isolated either after papain treatment or after solubilization with detergent, is identical to beta(2)-microglobulin, a protein previously isolated from human urine and shown to be homologous in structure to constant region domains of immunoglobulins. Moreover, quantitative data indicate virtually total identity between the small subunit of HL-A antigens and beta(2)-microglobulin. Studies of the turnover of labeled HL-A antigens from the lymphocyte surface indicate that the two subunits turn over at similar rates, although only the small subunit could be detected in the culture medium. The significance of these observations is discussed.
已采用多种免疫学方法来表明，经木瓜蛋白酶处理后或用去污剂溶解后分离得到的HL-A抗原的小亚基，与β2-微球蛋白相同，β2-微球蛋白是一种先前从人尿中分离出来的蛋白质，其结构与免疫球蛋白恒定区结构域同源。此外，定量数据表明HL-A抗原的小亚基与β2-微球蛋白几乎完全相同。对淋巴细胞表面标记的HL-A抗原周转的研究表明，尽管在培养基中只能检测到小亚基，但两个亚基的周转速度相似。讨论了这些观察结果的意义。
