期刊
GLYCOCONJUGATE JOURNAL
卷 23, 期 5-6, 页码 345-354出版社
SPRINGER
DOI: 10.1007/s10719-006-6693-4
关键词
Drosophila melanogaster; mass spectrometry; glycomics; sialic acid
资金
- NIGMS NIH HHS [R01 GM069952] Funding Source: Medline
- Wellcome Trust Funding Source: Medline
With the complete genome sequence of Drosophila melanogaster defined a systematic approach towards understanding the function of glycosylation has become possible. Structural assignment of the entire Drosophila glycome during specific developmental stages could provide information that would shed further light on the specific roles of different glycans during development and pinpoint the activity of certain glycosyltransferases and other glycan biosynthetic genes that otherwise might be missed through genetic analyses. In this paper the major glycoprotein N- and O-glycans of Drosophila embryos are described as part of our initial undertaking to characterize the glycome of Drosophila melanogaster. The N-glycans are dominated by high mannose and paucimannose structures. Minor amounts of mono-, bi- and tri-antennary complex glycans were observed with GlcNAc and Gal beta 1-4GlcNAc non-reducing end termini. O-glycans were restricted to the mucin-type core 1 Gal beta 1-3GalNAc sequence.
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