Durda P J, Boos S C, Gottlieb P D
J Immunol. 1979 Apr;122(4):1407-12.
A cell surface glycoprotein (designated T100) of apparent m.w. 100,000 by SDS-PAGE under reducing and nonreducing conditions was precipitated from NP-40 extracts of surface radiolabeled thymocytes from a variety of inbred strains of mice by the standard noncongenic Lyt-2.1-typing serum. The inbred stain distribution, trypsin sensitivity on intact cells, and apparent m.w. of T100 suggest that it is different from Lyt-2.1. Inheritance and expression of T100 suggest that it is determined by an allele at a single locus, and testing of CXB recombinant inbred strains and B6.C minor histocompatibility congenic strains suggest that this locus is linked to H-25. Antiserum absorption experiments, two-stage cytotoxicity assays, and results of immunoprecipitations performed after prebinding antibody to radiolabeled thymocytes suggest that some T100 is accessible to antibody on the intact cell surface. However, for unknown reasons the number of cells required to absorb anti-T100 precipitating activity from antiserum was much higher than for removal of anti-Lyt-2.1 activity. A molecule with properties of T100 was also detected on lymph node cells and on the AKTB-1 lymphoma.
在还原和非还原条件下,通过SDS-PAGE测定,一种表观分子量为100,000的细胞表面糖蛋白(命名为T100)可被标准的非同源Lyt-2.1分型血清从多种近交系小鼠的表面放射性标记胸腺细胞的NP-40提取物中沉淀出来。T100的近交系分布、完整细胞上的胰蛋白酶敏感性以及表观分子量表明它与Lyt-2.1不同。T100的遗传和表达表明它由单个基因座上的一个等位基因决定,对CXB重组近交系和B6.C次要组织相容性同源系的检测表明该基因座与H-25连锁。抗血清吸收实验、两阶段细胞毒性测定以及在将抗体预结合到放射性标记胸腺细胞后进行的免疫沉淀结果表明,完整细胞表面的一些T100可被抗体识别。然而,出于未知原因,从抗血清中吸收抗T100沉淀活性所需的细胞数量远高于去除抗Lyt-2.1活性所需的细胞数量。在淋巴结细胞和AKTB-1淋巴瘤上也检测到了具有T100特性的分子。