Marchalonis J J
Science. 1975 Oct 3;190(4209):20-9. doi: 10.1126/science.1101378.
Immunoglobulins have been isolated from the surface of B (bone marrow-derived) and T (thymus-derived) lymphocytes. Two types of membrane immunoglobulin occur on B lymphocytes; one type resembles the 200,000-dalton subunit of IgM, the second possesses a heavy chain electrophoretically distinct from mu chain and does not correspond to any of the known classes of mouse immunoglobulins. It might correspond to human sigma chain. T lymphocytes possess only one type of surface immunoglobulin. This molecule has a mass of approximately 200,000 daltons and contains light chains and heavy chains similar to, but not identical to, mu chains. Evidence now exists that surface IgM-like immunoglobulins of B lymphocytes and T lymphocytes activated to certain antigens can bind specifically to antigen. These observations suggest that surface immunoglobulin functions as a receptor for antigen on B cells and at least on some T cells. The mechanisms by which combination of antigen with surface immunoglobulin initiate differentiation remain to be determined.
免疫球蛋白已从B(骨髓来源)淋巴细胞和T(胸腺来源)淋巴细胞表面分离出来。B淋巴细胞上存在两种膜免疫球蛋白;一种类似于IgM的200,000道尔顿亚基,另一种具有一条在电泳上与μ链不同的重链,且与任何已知的小鼠免疫球蛋白类别都不对应。它可能对应于人类的σ链。T淋巴细胞仅有一种表面免疫球蛋白。该分子质量约为200,000道尔顿,含有与μ链相似但不完全相同的轻链和重链。现在有证据表明,被某些抗原激活的B淋巴细胞和T淋巴细胞的表面IgM样免疫球蛋白可特异性结合抗原。这些观察结果表明,表面免疫球蛋白在B细胞以及至少某些T细胞上作为抗原受体发挥作用。抗原与表面免疫球蛋白结合引发分化的机制仍有待确定。