{"refrec":{"BRefID":280834,"RR":"<b>Siddiqui, N.I.; Idakieva, K.; Demarsin, B.; Doumanova, L.; Compernolle, F.; Gielens, C.</b> (2007). Involvement of glycan chains in the antigenicity of <i>Rapana thomasiana</i> hemocyanin. <i>Biochem. Biophys. Res. Commun. 361(3)</i>: 705-711. <a href=\"https://dx.doi.org/10.1016/j.bbrc.2007.07.098\" target=\"_blank\">https://dx.doi.org/10.1016/j.bbrc.2007.07.098</a>","BEntID":272853,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":1,"RefStringPartII":". <i>Biochem. Biophys. Res. Commun. 361(3)</i>: 705-711. <a href=\"https://dx.doi.org/10.1016/j.bbrc.2007.07.098\" target=\"_blank\">https://dx.doi.org/10.1016/j.bbrc.2007.07.098</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Siddiqui, N.I.; Idakieva, K.; Demarsin, B.; Doumanova, L.; Compernolle, F.; Gielens, C.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Siddiqui, N.I. <i>et al.</i>","Englishabstract":"Functional unit (FU) <i>Rt</i>H2-<i>e</i> from <i>Rapana thomasiana</i> hemocyanin (Hc) was degraded into small fragments with chymotrypsin. The glycopeptides were separated from the non-glycosylated peptides by chromatography on Concanavalin-A–Sepharose and characterized by mass spectrometry. The glycan part of the glycopeptides (all with common peptide stretch of 14 amino acids) consists of the classical trimannosyl-<i>N,N</i>-diacetylchitobiose core for <i>N</i>-glycosylation, predominantly extended with a unique tetrasaccharide that is branched on fucose. In inhibition ELISA experiments, the glycopeptides interfered in the complex formation between FU <i>Rt</i>H2-<i>e</i> and rabbit antibodies against <i>Rapana</i> Hc (about 30% of inhibition). The inhibition also was retained after treatment of the glycopeptides with pronase in order to completely destroy the peptide part. The inhibitory effect of the non-glycosylated peptides, on the other hand, was very low. 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