Pischel K D, Little J R
J Immunol. 1979 May;122(5):1821-7.
Immunochemical studies of murine thymus-leukemia antigens (TLA) have confirmed that the subunit structure consists of a 45,000-dalton heavy chain and a beta 2 microglobulin (beta 2m) light chain. Similar structural features are exhibited by the TLA from thymocytes of Tlaa, Tlac, Tlad, and a leukemia cell derived from C57BL/6, a Tlab strain. In addition to the similar subunit structure from the four haplotypes, each TLA shows a similar pattern of trypsin proteolysis. This procedure yields a major heavy chain cleavage product of approximately 37,000 daltons that remains associated with beta 2m and retains most or all of the antigenic determinants of the intact TLA. Evidence is presented that TLA do not exhibit Fc receptor properties, nor do they adsorb to murine leukemia virus antigens under the conditions of isolation for analysis on polyacrylamide gel electrophoresis (PAGE) in sodium dodecyl sulfate (SDS). Taken together these findings strongly support the hypothesis that TLA comprise a family of chemically similar antigens belonging to a structurally and genetically related group that includes H-2D, H-2K, and Qa-2,3.
对小鼠胸腺白血病抗原（TLA）的免疫化学研究证实，其亚基结构由一条45,000道尔顿的重链和一条β2微球蛋白（β2m）轻链组成。来自Tlaa、Tlac、Tlad的胸腺细胞以及源自Tlab品系C57BL/6的白血病细胞的TLA也表现出类似的结构特征。除了这四种单倍型具有相似的亚基结构外，每种TLA还呈现出相似的胰蛋白酶蛋白水解模式。该过程产生一种约37,000道尔顿的主要重链裂解产物，该产物仍与β2m结合，并保留了完整TLA的大部分或全部抗原决定簇。有证据表明，TLA不表现出Fc受体特性，在十二烷基硫酸钠（SDS）聚丙烯酰胺凝胶电泳（PAGE）分析的分离条件下，它们也不吸附小鼠白血病病毒抗原。综合这些发现有力地支持了这样一种假设，即TLA构成了一类化学性质相似的抗原家族，属于一个结构和遗传相关的群体，其中包括H-2D、H-2K和Qa-2、3。
