{"refrec":{"BRefID":280732,"RR":"<b>Velkova, L.; Dolashka, P.; Lieb, B.; Dolashki, A.; Voelter, W.; Van Beeumen, J.; Devreese, B.</b> (2011). Glycan structures of the structural subunit (HtH1) of <i>Haliotis tuberculata</i> hemocyanin. <i>Glycoconjugate Journal 28(6)</i>: 385-395. <a href=\"https://dx.doi.org/10.1007/s10719-011-9337-2\" target=\"_blank\">https://dx.doi.org/10.1007/s10719-011-9337-2</a>","BEntID":272751,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":1,"RefStringPartII":". <i>Glycoconjugate Journal 28(6)</i>: 385-395. <a href=\"https://dx.doi.org/10.1007/s10719-011-9337-2\" target=\"_blank\">https://dx.doi.org/10.1007/s10719-011-9337-2</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Velkova, L.; Dolashka, P.; Lieb, B.; Dolashki, A.; Voelter, W.; Van Beeumen, J.; Devreese, B.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Velkova, L. <i>et al.</i>","Englishabstract":"The oligosaccharide structures of the structural subunit HtH1 of <i>Haliotis tuberculata</i> hemocyanin (HtH) were studied by mass spectral sequence analysis of the glycans. The proposed structures are based on MALDI-TOF-MS data before and after treatment with the specific exoglycosidases β1-3,4,6-galactosidase and <i>α</i>1-6(>2,3,4) fucosidase followed by sequence analysis via electrospray ionization MS/MS-spectra. In total, 15 glycans were identified as a highly heterogeneous group of structures. As in most molluscan hemocyanins, the glycans of HtH1 contain a terminal MeHex, but more interestingly, a novel structural motif was observed: MeHex[Fuc(<i>α</i>1-3)-]GlcNAc, including thus MeHex and (<i>α</i>1-3)-Fuc residues being linked to an internal GlcNAc residue. While the functional unit (FU) c (HtH1-c) is completely lacking any potential glycosylation site, FU-h possesses a second exposed sugar attachment site between beta-strands 8 and 9 within the beta sandwich domain compared to the other FUs. The glycosylation pattern/sites show a high degree of conservation. In FU-h two prominent potential glycosylation sites can be detected. The finding that HtH1 is not able to form multidecameric structures <i>in vivo</i> could be explained by the presence of the exposed glycan on the surface of FU-h.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"Glycan structures of the structural subunit (HtH1) of <i>Haliotis tuberculata</i> hemocyanin","OrigTitleLangCode":"en","OrigTitleLangCodeExtended":"eng","OrigTitleLangID":15,"DateLastModified":{"date":"2024-12-10 01:33:17.368041","timezone_type":1,"timezone":"+01:00"},"UserAccessRight":null,"UserAccID":null,"AuthorKeywords":"Electrospray ionization; Haliotis tuberculata; Hemocyanin; Massspectrometry; Oligosaccharide structures","OtherDescriptors":null,"Notes":null,"AnaPub":2011,"MonPub":null,"DateUpdate":"2022-05-03","DateCreate":"2016-10-09","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000293641700002","VABBcode":null,"OpenAcc":0,"DOI":"10.1007/s10719-011-9337-2"},"refs":null,"anarec":{"AnaID":280732,"PubliDate":2011,"Pagination":"385-395","XtraPublOfAnaID":null,"ISBN":null,"Volume":"28","Issue":"6","BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":268803,"SerRR":"Glycoconjugate Journal. 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