Charron D J, Aellen-Schulz M F, St Geme J, Erlich H A, McDevitt H O
Mol Immunol. 1983 Jan;20(1):21-32. doi: 10.1016/0161-5890(83)90101-3.
Ii, a 31,000 mol. wt polypeptide chain associated with murine and human Ia antigens was investigated for its labeling pattern, carbohydrate content and structural polymorphism. Two-dimensional gel electrophoretic analysis of tunicamycin treated cells from mouse and human lymphocytes shows that Ii contains two N-linked carbohydrate chains. Ii is a methionine rich polypeptide. Tryptic and chymotryptic two dimensional peptide maps of Ii chain associated with I-A and I-E subregion products are identical. This absence of polymorphism holds true when Ii chain is isolated from different mouse haplotypes. Human Ii chains from different HLA-DR types appear also invariant by peptide map analysis. By molecular weight, carbohydrate content, charge and tryptic and chymotryptic maps criteria, Ii of mouse and human are strikingly homologous.
对与小鼠和人类Ia抗原相关的一条分子量为31,000的多肽链的标记模式、碳水化合物含量和结构多态性进行了研究。对来自小鼠和人类淋巴细胞的衣霉素处理细胞进行二维凝胶电泳分析表明，Ii含有两条N-连接的碳水化合物链。Ii是一种富含甲硫氨酸的多肽。与I-A和I-E亚区产物相关的Ii链的胰蛋白酶和糜蛋白酶二维肽图是相同的。当从不同的小鼠单倍型中分离出Ii链时，这种多态性的缺失仍然成立。通过肽图分析，来自不同HLA-DR类型的人类Ii链也表现出不变性。根据分子量、碳水化合物含量、电荷以及胰蛋白酶和糜蛋白酶图谱标准，小鼠和人类的Ii具有显著的同源性。
