The invariant chain of murine Ia antigens: its glycosylation, abundance and subcellular localization.
The invariant chain of murine Ia antigens: its glycosylation, abundance and subcellular localization.
复制标题
鼠 Ia 抗原的不变链：其糖基化、丰度和亚细胞定位。
DOI：
10.1016/0161-5890(81)90013-4
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发表时间：
1981
影响因子：
3.6
通讯作者：
Jones,PP
中科院分区：
文献类型：
--
作者：
Sung,E;Jones,PP
研究了不变Ia抗原相关多肽链(II)的性质。从衣霉素处理的小鼠脾细胞免疫沉淀的Ia抗原的二维凝胶分析被用来鉴定IAS的非糖基化多肽前体及其I-A和I-E亚区控制链。结果表明，I含有两个N-连接的碳水化合物单元。也有证据表明，在提取过程中，亚胺不与Ia结合，细胞中可能存在一个不与多态链结合的游离亚胺池。仅从细胞表面表达的Ia分子亚群或从分离的质膜中免疫沉淀Ia抗原表明，这些制剂中不存在Iita抗原。由于IIIs存在于细胞膜中，而不是游离在细胞质中，因此，IIIis可能与细胞内膜上的Ia链多态有关，而不是与细胞表面的Ia链有关。
The properties of the invariant Ia antigen-associated polypeptide chain (Ii) have been examined. Two-dimensional gel analysis of Ia antigens immunoprecipitated from tunicamycin-treated murine spleen cells has been employed to identify the non-glycosylated polypeptide precursors for Iias well as for theI-AandI-ESubregion controlled chains. The results indicate that Iicontains two N-linked carbohydrate units. Evidence is also presented that Iidoes not bind adventitiously to Ia during extraction procedures and that a pool of free Iimay exist in the cell which is not bound to the polymorphic chains. Immunoprecipitation of Ia antigens from only the cell surface-expressed subset of Ia molecules or from isolated plasma membrane shows Iito be absent from these preparations. Since Iiis found in cellular membranes but not free in the cytosol, it seems likely that Iiis associated with the polymorphic Ia chains in the intracellular membranes but not on the cell surface.