Freed J H, David C S, Shreffler D C, Nathenson S G
J Immunol. 1978 Jul;121(1):91-7.
Ia antigens from the I-A8 and I-Ck subregions of the B10.HTT (H-2t3) strain of mice were isolated by indirect immunoprecipitation of arginine-labeled, nonionic detergent-solubilized materials. After biochemical purification the electrophoretically homogeneous 28,000 dalton glycoprotein beta chains from the Ia precipitates were digested with trypsin and the resultant radiolabeled tryptic peptides were compared by analytical ion exchange chromatography. These comparisons reveal that the beta chains of Ia antigens from the A (I-A8) and C (I-Ck) subregions of B10.HTT share only two out of 12 to 14 of their arginine tryptic peptides. Thus these noncross-reactive Ia antigens are structurally quite diverse, and would possess sufficient structural variability to account for their lack of antigenic cross-reactivity.
通过对用精氨酸标记、非离子去污剂增溶的物质进行间接免疫沉淀，从小鼠B10.HTT（H-2t3）品系的I-A8和I-Ck亚区分离出Ia抗原。经过生化纯化后，对Ia沉淀物中电泳均一的28,000道尔顿糖蛋白β链用胰蛋白酶进行消化，并用分析离子交换色谱法比较所得的放射性标记胰蛋白酶肽。这些比较表明，B10.HTT的A（I-A8）和C（I-Ck）亚区的Ia抗原的β链在其12至14个精氨酸胰蛋白酶肽中仅共有两个。因此，这些非交叉反应性Ia抗原在结构上差异很大，并且具有足够的结构变异性来解释它们缺乏抗原交叉反应性的原因。
