人Ig - A1和IgA2免疫球蛋白中寡糖的位置及结构意义
Location and structural significance of the oligosaccharides in human Ig-A1 and IgA2 immunoglobulins.
作者信息
Toraño A, Tsuzukida Y, Liu Y S, Putnam F W
出版信息
Proc Natl Acad Sci U S A. 1977 Jun;74(6):2301-5. doi: 10.1073/pnas.74.6.2301.
Abstract
The location, number, and kinds of oligosaccharides in human IgA1 and IgA2 immunoglobulins have been determined by amino acid sequence analysis of the alpha heavy chains. Both A2m allotypes of the alpha2 chain of IgA2 have two GlcN oligosaccharides that are absent in the alpha1 chain, but they lack GalN. The A2m(2) allotype has a fifth GlcN oligosaccharide. The alpha chains of IgA proteins also have subclass-specific and allotype-specific differences in amino acid sequence. Although other classes of human immunoglobulins differ in the number and kind of oligosaccharides, the sites are often homologous and are related to the immunoglobulin domain structure. Evolutionary preservation of the tripeptide acceptor sequence for GlcN probably indicates both a structural and biological role for carbohydrate.
摘要
通过对α重链进行氨基酸序列分析，已确定人IgA1和IgA2免疫球蛋白中寡糖的位置、数量和种类。IgA2的α2链的两种A2m同种异型均有两个在α1链中不存在的GlcN寡糖，但它们缺乏GalN。A2m(2)同种异型有第五个GlcN寡糖。IgA蛋白的α链在氨基酸序列上也存在亚类特异性和同种异型特异性差异。尽管人类其他类别的免疫球蛋白在寡糖的数量和种类上有所不同，但这些位点通常是同源的，并且与免疫球蛋白结构域结构相关。GlcN三肽受体序列的进化保守性可能表明碳水化合物具有结构和生物学作用。
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