从被激活以识别组织相容性抗原的胸腺细胞中分离出的细胞表面免疫球蛋白的抗原结合特异性。
Antigen-binding specificity of isolated cell-surface immunoglobulin from thymus cells activated to histocompatibility antigens.
作者信息
Cone R E, Sprent J, Marchalonis J J
出版信息
Proc Natl Acad Sci U S A. 1972 Sep;69(9):2556-60. doi: 10.1073/pnas.69.9.2556.
Abstract
Lactoperoxidase-catalyzed radioiodination of cell-surface proteins was used in the isolation of cell-surface immunoglobulin from thymus-derived thoracic duct lymphocytes activated to histocompatibility-2 antigens. Immunoglobulin was identified by specific precipitation with antiserum to mouse immunoglobulin. Polyacrylamide gel electrophoresis of reduced and alkylated precipitates showed that the immunoglobulin molecules possessed mu-type heavy chains and light chains. Cell-surface immunoglobulin isolated from thymus-derived cells activated to histocompatibility-2 antigens possessed binding specificity for the activating antigens.
摘要
乳过氧化物酶催化的细胞表面蛋白放射性碘化被用于从被激活以识别组织相容性-2抗原的胸腺来源的胸导管淋巴细胞中分离细胞表面免疫球蛋白。通过用抗小鼠免疫球蛋白抗血清进行特异性沉淀来鉴定免疫球蛋白。还原和烷基化沉淀物的聚丙烯酰胺凝胶电泳表明，免疫球蛋白分子具有μ型重链和轻链。从被激活以识别组织相容性-2抗原的胸腺来源细胞中分离出的细胞表面免疫球蛋白对激活抗原具有结合特异性。
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