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- aggregation classification "A1".
- aggregation creator B448624.
- aggregation creator B448625.
- aggregation creator B448626.
- aggregation creator B448627.
- aggregation creator B448628.
- aggregation creator person.
- aggregation creator person.
- aggregation date "2011".
- aggregation format "application/pdf".
- aggregation hasFormat 2040309.bibtex.
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- aggregation hasFormat 2040309.doc.
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- aggregation isPartOf urn:issn:0282-0080.
- aggregation language "eng".
- aggregation rights "I have transferred the copyright for this publication to the publisher".
- aggregation subject "Biology and Life Sciences".
- aggregation title "Glycan structures of the structural subunit (HtH1) of Haliotis tuberculata hemocyanin".
- aggregation abstract "The oligosaccharide structures of the structural subunit HtH1 of Haliotis tuberculata 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 beta 1-3,4,6-galactosidase and alpha 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(alpha 1-3)-]GlcNAc, including thus MeHex and (alpha 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 in vivo could be explained by the presence of the exposed glycan on the surface of FU-h.".
- aggregation authorList BK782107.
- aggregation endPage "395".
- aggregation issue "6".
- aggregation startPage "385".
- aggregation volume "28".
- aggregation aggregates 2040321.
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