Carbohydrate of the human plasminogen variants. III. Structure of the O-glycosidically linked oligosaccharide unit.
Carbohydrate of the human plasminogen variants. III. Structure of the O-glycosidically linked oligosaccharide unit.
复制标题
人纤溶酶原变体的碳水化合物。
DOI：
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发表时间：
1979
影响因子：
4.8
通讯作者：
F. Castellino
中科院分区：
文献类型：
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作者：
M. L. Hayes;F. Castellino
本期的前两份手稿(Hayes，M.L.，和Castellino，F.J.(1979)J.Biol)。化学。254,8768-8771,8772-8776)描述了从人纤溶酶原亲和层析变异体1和2中分离和鉴定糖肽。纤溶酶原变异体1包含一个基于天冬酰胺288的分支碳水化合物结构，该结构已在前一篇手稿中建立。这种结构在变异体2中不存在。纤溶酶原变异体1和2含有基于苏氨酸的糖偶联物。这种后一种结构是通过结合甲基化数据、糖苷酶消化、高碘酸盐氧化和β-消除的还原寡糖的Smith降解来建立的。从纤溶酶原变异体1(1D)和2(2D)中分离得到一个糖肽单位，其结构如下：SIAα2产生3Galβ1产生3GalNAc-Thr。苏氨酸是Glu-纤溶酶原序列中的第345位残基。在变异体1(1E)和变异体2(2E)中也发现了另一个糖肽单位，产量较低。该单元的结构为：Siaα2得3GalBeta1，得3GalNAc-Thr。：FORMULA：(见正文)，Alpha 2，6 Sia。同样，Thr345是糖基化氨基酸。糖基化苏氨酸周围的氨基酸序列为NH2-Ala.Pro.Thr(CHO).Ala.Pro.Pro.Glu。
The preceding two manuscripts in this issue (Hayes, M. L., and Castellino, F. J. (1979) J. Biol. Chem. 254, 8768-8771, 8772-8776) describe the isolation and characterization of glycopeptides from human plasminogen affinity chromatography variants 1 and 2. Plasminogen variant 1 contains an asparagine288-based branched carbohydrate structure, which has been established in the immediately preceding manuscript. This structure is absent in variant 2. Plasminogen variants 1 and 2 contain a threonine-based glycoconjugate. This latter structure has been established by combination of methylation data, glycosidase digestions, periodate oxidations, and Smith degradations of the beta-eliminated reduced oligosaccharides. One glycopeptide unit, isolated from both plasminogen variants 1 (1D) and 2 (2D) possessed the following structure: Sia alpha 2 yields 3Gal beta 1 yields 3GalNAc-Thr. The threonine was found to be residue 345 in the Glu-plasminogen sequence. Another glycopeptide unit was also found to be present, in lower yields in both variants 1 (1E) and 2 (2E). The structure of this unit was: Sia alpha 2 yields 3Gal beta1 yields 3GalNAc-Thr. : formula: (see text), alpha 2,6 Sia. Again Thr 345 was the glycosylated amino acid. The amino acid sequence around the glycosylated threonine was found to be NH2-Ala.Pro.Thr(CHO).Ala.Pro.Pro.Glu.