Over het archief
Het OWA, het open archief van het Waterbouwkundig Laboratorium heeft tot doel alle vrij toegankelijke onderzoeksresultaten van dit instituut in digitale vorm aan te bieden. Op die manier wil het de zichtbaarheid, verspreiding en gebruik van deze onderzoeksresultaten, alsook de wetenschappelijke communicatie maximaal bevorderen.
Dit archief wordt uitgebouwd en beheerd volgens de principes van de Open Access Movement, en het daaruit ontstane Open Archives Initiative.
Basisinformatie over ‘Open Access to scholarly information'.
Mass spectral evidence for N-glycans with branching on fucose in a molluscan hemocyanin
Gielens, C.; Idakieva, K.; Van den Bergh, V.; Siddiqui, N.I.; Parvanova, K.; Compernolle, F. (2005). Mass spectral evidence for N-glycans with branching on fucose in a molluscan hemocyanin. Biochem. Biophys. Res. Commun. 331(2): 562-570. https://dx.doi.org/10.1016/j.bbrc.2005.03.217
In: Biochemical and Biophysical Research Communications. ACADEMIC PRESS INC ELSEVIER SCIENCE: San Diego etc.. ISSN 0006-291X; e-ISSN 1090-2104, meer
|  |
| Trefwoorden |
Gastropoda [WoRMS]; Mollusca [WoRMS]; Rapana thomasiana Crosse, 1861 [WoRMS]
Marien/Kust |
| Author keywords |
deglycosylation; electrospray ionization mass spectrometry; fucose; gaschromatography; gastropod; hemocyanin; mollusc; MS/MS; N-glycosylation;Rapana thomasiana |
| Auteurs | | Top |
- Gielens, C., meer
- Idakieva, K.
- Van den Bergh, V.
|
- Siddiqui, N.I.
- Parvanova, K.
- Compernolle, F.
|
|
| Abstract |
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. |
IMIS is ontwikkeld en wordt gehost door het VLIZ.
