{"refrec":{"BRefID":280936,"RR":"<b>Gielens, C.; Idakieva, K.; Van den Bergh, V.; Siddiqui, N.I.; Parvanova, K.; Compernolle, F.</b> (2005). Mass spectral evidence for <i>N</i>-glycans with branching on fucose in a molluscan hemocyanin. <i>Biochem. Biophys. Res. Commun. 331(2)</i>: 562-570. <a href=\"https://dx.doi.org/10.1016/j.bbrc.2005.03.217\" target=\"_blank\">https://dx.doi.org/10.1016/j.bbrc.2005.03.217</a>","BEntID":272955,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":1,"RefStringPartII":". <i>Biochem. Biophys. Res. Commun. 331(2)</i>: 562-570. <a href=\"https://dx.doi.org/10.1016/j.bbrc.2005.03.217\" target=\"_blank\">https://dx.doi.org/10.1016/j.bbrc.2005.03.217</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Gielens, C.; Idakieva, K.; Van den Bergh, V.; Siddiqui, N.I.; Parvanova, K.; Compernolle, F.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Gielens, C. <i>et al.</i>","Englishabstract":"Glycopeptides, isolated from a trypsinolysate of functional unit (FU) <i>Rt</i>H2-<i>e</i> of <i>Rapana thomasiana</i> 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 <i>Rt</i>H2-<i>e</i> with a glycosylation site at Asn-127. Besides the core structure Man<sub>3</sub>GlcNAc<sub>2</sub> 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-<i>O</i>-methylgalactose and <i>N</i>-acetylgalactosamine, and linked to GlcNAc at the reducing end. This structure represents a novel <i>N</i>-glycan motif and is likely to be immunogenic. 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