Cone R E, Takeda A, Beaman K D, Ferguson T A, Iverson G M
Department of Pathology, Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, Conn.
Exp Clin Immunogenet. 1986;3(4):208-18.
T-cell antigen binding molecules (TABM) specific for trinitrophenol (TNP), oxazalone, azobenzenearsonate or sheep erythrocytes were purified by affinity to antigen, adsorption to monoclonal antibodies to antigen binding molecules or were synthesized by translation of immunopurified mRNA for TABM in vitro. These molecules and a T-cell line, BW5147, membrane protein bound by rabbit antibodies to TABM were radiolabeled by 125I, digested with Staphylococcus V8 protease, and peptides of the proteolytic digest were resolved by 2D-gel peptide mapping. Comparison of the peptide maps of these proteins and amino acid analysis of T-cell antigen binding molecules specific for TNP or sheep erythrocytes indicate similarities and distinctions suggesting variable and constant domains in these molecules.
对三硝基苯酚（TNP）、恶唑酮、偶氮苯砷酸盐或绵羊红细胞具有特异性的T细胞抗原结合分子（TABM），通过与抗原的亲和力、对抗原结合分子的单克隆抗体吸附进行纯化，或通过体外翻译免疫纯化的TABM mRNA进行合成。这些分子以及一个T细胞系BW5147（其膜蛋白被抗TABM的兔抗体所结合）用125I进行放射性标记，用葡萄球菌V8蛋白酶消化，蛋白水解消化产生的肽段通过二维凝胶肽图谱进行分离。这些蛋白质的肽图谱比较以及对TNP或绵羊红细胞具有特异性的T细胞抗原结合分子的氨基酸分析表明了相似性和差异，提示这些分子中存在可变区和恒定区。
