کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10769987 | 1050827 | 2005 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Mass spectral evidence for N-glycans with branching on fucose in a molluscan hemocyanin
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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![عکس صفحه اول مقاله: Mass spectral evidence for N-glycans with branching on fucose in a molluscan hemocyanin Mass spectral evidence for N-glycans with branching on fucose in a molluscan hemocyanin](/preview/png/10769987.png)
چکیده انگلیسی
Glycopeptides, isolated from a trypsinolysate of functional unit (FU) RtH2-e of Rapana thomasiana hemocyanin subunit 2, were analysed by electrospray ionization mass spectrometry and MS/MS. From the molecular mass observed after deglycosylation, it was inferred that all glycopeptides shared the same peptide stretch 92-143 of FU RtH2-e with a glycosylation site at Asn-127. Besides the core structure Man3GlcNAc2 for N-glycosylation, structures with a supplementary GlcNAc linked to either the Man(α1-3) or the Man(α1-6) arm and/or an additional tetrasaccharide unit connected to the other Man arm were observed, indicating the existence of microheterogeneity at the glycan level. The tetrasaccharide unit contains a central fucose moiety substituted with 3-O-methylgalactose and N-acetylgalactosamine, and linked to GlcNAc at the reducing end. This structure represents a novel N-glycan motif and is likely to be immunogenic. A second potential site for N-glycosylation in FU RtH2-e at Asn-17 was shown to be not glycosylated.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 331, Issue 2, 3 June 2005, Pages 562-570
Journal: Biochemical and Biophysical Research Communications - Volume 331, Issue 2, 3 June 2005, Pages 562-570
نویسندگان
Constant Gielens, Krassimira Idakieva, Viviane Van den Bergh, Nurul I. Siddiqui, Katja Parvanova, Frans Compernolle,