Haustein D, Günther E
Eur J Immunol. 1980 Aug;10(8):615-20. doi: 10.1002/eji.1830100808.
The gene products of the A and B regions of the rat major histocompatibility system (RT1) have been analyzed by immunoprecipitation and sodium dodecyl sulfate polyacrylamide gel electrophoresis. For antiserum production and as a source of target spleen cells, rat strains were used that differed only for various combinations of the RT1 regions. It could be shown that te RT1.A region, whose serologically detectable products behave like classical transplantation antigens, coded for molecules of 45 000 daltons that were associated with 12 500 dalton molecules. The RT1.B region products, which behave serologically like Ia antigens, consisted of two chains of 31 000 and 27 000 daltons, respectively. Thus, serological and biochemical phenotypes of the RT1 antigens could be matched in accordance with data obtained in other species and could be assigned to particular regions of the RT1 system. The two-peak structure of Ia antigens was only detectable under nonreducing conditions. After reduction, both peaks fused, presumably due to cleavage of intrachain disulfide bonds in the smaller chain.
通过免疫沉淀和十二烷基硫酸钠聚丙烯酰胺凝胶电泳对大鼠主要组织相容性系统(RT1)A区和B区的基因产物进行了分析。为了制备抗血清以及作为靶脾细胞的来源,使用了仅在RT1区域的各种组合上存在差异的大鼠品系。结果表明,RT1.A区的血清学可检测产物表现得像经典移植抗原,编码45000道尔顿的分子,这些分子与12500道尔顿的分子相关联。RT1.B区的产物在血清学上表现得像Ia抗原,分别由两条31000道尔顿和27000道尔顿的链组成。因此,RT1抗原的血清学和生化表型可以根据在其他物种中获得的数据进行匹配,并可以指定到RT1系统的特定区域。Ia抗原的双峰结构仅在非还原条件下可检测到。还原后,两个峰融合,推测是由于较小链中的链内二硫键断裂。