期刊
JOURNAL OF PROTEOME RESEARCH
卷 8, 期 2, 页码 546-555出版社
AMER CHEMICAL SOC
DOI: 10.1021/pr800725v
关键词
-
资金
- International Foundation for Sciences [AB/19085]
- Wellcome Trust
- Biotechnology and Biological Sciences Research Council
The extracellular domain of E2 glycoprotein outer surface of the classical swine fever virus was expressed in epithelial kidney pig cells. The N-glycosylation determined by combination of Normal Phase-HPLC, Weak Anion Exchange-HPLC, exoglycosidase digestions and Mass Spectrometry revealed a complex mixture of neutral and monosialylated multiantennary N-glycans with variable number of alpha 1-3-Gal-Gal antennae terminals. The most abundant neutral N-glycan has a composition of HeX(7)HexNAC4dHexl, Negative ion ESI-MS/MS confirmed the presence of the 0-3-Gal-Gal motif on each arm of the fucosylated biantennary N-glycan. The most abundant monosialylated glycan was HeX6HexNAC4d Hex, Neu5Acl, with the sialic acid linked to the terminal fl1-4-Gal-G1cNAc. Sialic acid on the antenna capping position was predominantly of the N-acetyl form.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据