Yokoyama K, Stockert E, Old L J, Nathenson S G
Immunogenetics. 1982;15(6):543-9. doi: 10.1007/BF00347048.
Comparative tryptic peptide mapping and partial amino-terminal primary sequence analysis of the light chain component associated with the TL antigens showed that the small subunit of TL was identical to the beta 2m light chain associated with the H-2K or D product of the same strain. Peptide comparison of the beta 2m from the Tla products of an A strain X-ray induced leukemia RADA1 (Tlaa) and of a C57BL/6 strain X-ray induced leukemia ERLD (Tlab) showed differences to the extent of 25-35% in their peptides. This is consistent with previous results showing beta 2m allelic variations between these mouse strains. The data prove the structural identity of the beta 2m molecules from TL and H-2K, D antigens as well as reveal the strain specific polymorphism of the beta 2m associated with these products.
与TL抗原相关的轻链成分的比较胰蛋白酶肽图谱分析和部分氨基末端一级序列分析表明,TL的小亚基与同一品系的H-2K或D产物相关的β2m轻链相同。对A品系X射线诱导白血病RADA1(Tlaa)和C57BL/6品系X射线诱导白血病ERLD(Tlab)的Tla产物中的β2m进行肽比较,结果显示它们的肽差异程度为25%-35%。这与之前显示这些小鼠品系之间β2m等位基因变异的结果一致。这些数据证明了来自TL和H-2K、D抗原的β2m分子的结构同一性,同时也揭示了与这些产物相关的β2m的品系特异性多态性。