Moseley J M, Marchalonis J J, Harris A W, Pye J
J Immunogenet. 1977 Aug;4(4):233-48. doi: 10.1111/j.1744-313x.1977.tb00906.x.
Immunoglobulin (Ig) released into the medium by monoclonal continuously cultured murine T lymphoma cells of the lines WEHI-22 and WEHI-7 was isolated by serological precipitation or solid-phase immunoadsorption techniques. The intact immunoglobulin had an electrophoretic mobility on sodium dodecyl-sulphate (SDS) containing polyacrylamide gels comparable to that of IgG (mass 150,000). This mobility was significantly faster than that of '7S' IgM of murine B lymphocyte surfaces. The T lymphoma immunoglobulin consisted of a pair of heavy chains linked by disulphide bonds and light chains non-covalently bound to the heavy chains. The isolated heavy chains migrated slightly faster than the mu chains of MOPC 104E IgM. Some, but not all, antisera directed against mu chains of normal mouse serum IgM bound T lymphoma immunoglobulin apparently via a cross-reaction localized to the Fd fragment. These data indicate that immunoglobulin of T lymphoma cells and, presumably normal T lymphocytes, represents an immunoglobulin isotype which is distinct from those immunoglobulins found on the B cell surface.
通过血清学沉淀或固相免疫吸附技术，从连续培养的WEHI - 22和WEHI - 7系小鼠T淋巴瘤单克隆细胞释放到培养基中的免疫球蛋白（Ig）被分离出来。完整的免疫球蛋白在含十二烷基硫酸钠（SDS）的聚丙烯酰胺凝胶上的电泳迁移率与IgG（质量150,000）相当。这种迁移率明显快于小鼠B淋巴细胞表面的“7S”IgM。T淋巴瘤免疫球蛋白由通过二硫键连接的一对重链和非共价结合到重链上的轻链组成。分离出的重链迁移速度略快于MOPC 104E IgM的μ链。一些但并非所有针对正常小鼠血清IgM的μ链的抗血清显然通过定位于Fd片段的交叉反应与T淋巴瘤免疫球蛋白结合。这些数据表明，T淋巴瘤细胞以及大概正常T淋巴细胞的免疫球蛋白代表一种与在B细胞表面发现的那些免疫球蛋白不同的免疫球蛋白同种型。
