van Agthoven A, Terhorst C
J Immunol. 1982 Jan;128(1):426-32.
Charge heterogeneity of the human thymocyte antigen T6 was studied by isoelectric focusing and two-dimensional gel electrophoresis. The larger subunit of T6 (a 49,000 m.w. glycoprotein) contained several oligosaccharide side chains bearing up to 12 terminal sialic acids. When T6 antigens from 19 individual thymuses were analyzed, no differences in the isoelectric focusing patterns of the larger subunit could be detected. The larger subunit of the T6 antigen from MOLT-4 cells (52,000 m.w.) contained an extra oligosaccharide if compared with the T6 antigen from thymus or three other T leukemic cell lines. Two types of small subunits of T6 were found. In addition to a protein of m.w. 12,000, pI 5.5 identified as beta 2-microglobulin, a (m.w. 12,000, pI 7.0) nonglycosylated protein, was detected on two dimensional gels. This protein does not cross-react with beta 2-microglobulin, and its amount varied in different T6 preparations. The tissue distribution, the m.w. the association with beta 2-microglobulin, and the limited structural heterogeneity of T6 support the idea that T6 is the human homologue of the murine thymus leukemia antigen (TL).
通过等电聚焦和二维凝胶电泳研究了人类胸腺细胞抗原T6的电荷异质性。T6的较大亚基（一种分子量为49,000的糖蛋白）含有几个带有多达12个末端唾液酸的寡糖侧链。当分析来自19个个体胸腺的T6抗原时，未检测到较大亚基等电聚焦模式的差异。与来自胸腺或其他三种T白血病细胞系的T6抗原相比，来自MOLT-4细胞的T6抗原的较大亚基（分子量52,000）含有一个额外的寡糖。发现了两种类型的T6小亚基。除了一种分子量为12,
