Structural analysis of a new B-cell-differentiation antigen associated with products of the I-A subregion of the H-2 complex.
Structural analysis of a new B-cell-differentiation antigen associated with products of the I-A subregion of the H-2 complex.
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与 H-2 复合物 I-A 亚区产物相关的新 B 细胞分化抗原的结构分析。
DOI：
10.1073/pnas.78.7.4525
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发表时间：
1981
影响因子：
11.1
通讯作者：
Thorley-Lawson,D
中科院分区：
文献类型：
--
作者：
Huber,BT;Jones,PP;Thorley-Lawson,D
Ia.W39是H-2复合物的I-Ab亚区的私有特异性。它选择性地在B淋巴细胞亚群上表达，这在携带xid基因的新生正常小鼠和成年突变小鼠中不存在。免疫沉淀和一维NaDodSO 4/聚丙烯酰胺凝胶电泳表明，带有Ia.W39的分子由两个非共价连接的糖蛋白组成，表观Mr为33，000和28，000。抗Ia.W39血清不能预先清除Iab分子;然而，常规的同种抗I-Ab血清完全清除了Ia.W39。考虑到Ia.W39和常规Iab免疫沉淀物产生的相同二维凝胶模式，我们认为所有Ia分子都具有常规特异性，只有一个子集会另外表达Ia.W39。Ia.W39可能不是碳水化合物抗原，因为抗生素衣霉素对其表达没有影响。它可能是由未知分子与A α和A β复合物的缔合诱导的这些链上的构象决定簇。
Ia.W39 is a private specificity of the I-Ab subregion of the H-2 complex. It is selectively expressed on a subset of B lymphocytes that is absent in newborn normal and adult mutant mice carrying the xid gene. Immunoprecipitation and one-dimensional NaDodSO4/polyacrylamide gel electrophoresis showed that the molecule bearing Ia.W39 consists of two noncovalently linked glycoproteins of apparent Mr 33,000 and 28,000. Anti-Ia.W39 serum did not preclear the Iab molecule; however, the conventional allo-anti-I-Ab serum cleared Ia.W39 completely. In view of the identical two-dimensional gel pattern generated by the Ia.W39 and the conventional Iab immunoprecipitates, we believe that all Ia molecules bear the conventional specificities and only a subset would in addition express Ia.W39. Ia.W39 is probably not a carbohydrate antigen, because the antibiotic tunicamycin had no influence on its expression. It may be a conformational determinant on the A alpha and A beta complex induced by the association of an unknown molecule with these chains.