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• W2078382249 abstract "We have investigated the structure of the glycosylphosphatidylinositol (GPI) anchor and the O-linked glycan chains of the 40/45-kDa glycoprotein from the cell surface of the protozoan parasite Trypanosoma cruzi. This glycoconjugate is the major acceptor for sialic acid transferred by trans-sialidase of T. cruzi Y-strain, epimastigote form. The GPI anchor was liberated by treatment with hot alkali, and the phosphoinositol-oligosaccharide moiety was characterized and shown to have the following structure. AEP | Man α(1−2) Man α(1−2) Man α(1−6) Man α(1−4) GleN α(1− 6) Ins-1-phosphate Usually the glucosamine was 6-O-substituted with 2-aminoethylphosphonate, and 2-aminoethylphosphonate was also present on the third mannose residue distal to glucosamine, partially replacing the ethanolamine phosphate. The β-eliminated reduced oligosaccharide chains showed that two novel classes of O-linked N-acetylglucosamine oligosaccharide were present. The first series had the structures Galpβ1-3GlcNAc-ol; Galpβ1-6(Galpβ1-3)GlcNAc-ol; and Galpβ1-2Galpβ1-6(Galpβ1-3)GlcNAc-ol, whereas the other series had a 1-4 linkage to N-acetylglucosaminitol and had structures Galpβ1-4GlcNAc-ol, Galpβ1-6(Galpβ1-4)GlcNAc-ol, and Galpβ1-2Galpβ1-6(Galpβ1-4)GlcNAc-ol. We have also investigated the kinetics of in vitro sialylation of these O-linked oligosaccharides by the T. cruzi trans-sialidase and have shown that incorporation of one molecule of sialic acid hinders entry of a second molecule when two potential acceptor sites are present. We have investigated the structure of the glycosylphosphatidylinositol (GPI) anchor and the O-linked glycan chains of the 40/45-kDa glycoprotein from the cell surface of the protozoan parasite Trypanosoma cruzi. This glycoconjugate is the major acceptor for sialic acid transferred by trans-sialidase of T. cruzi Y-strain, epimastigote form. The GPI anchor was liberated by treatment with hot alkali, and the phosphoinositol-oligosaccharide moiety was characterized and shown to have the following structure. AEP | Man α(1−2) Man α(1−2) Man α(1−6) Man α(1−4) GleN α(1− 6) Ins-1-phosphate Usually the glucosamine was 6-O-substituted with 2-aminoethylphosphonate, and 2-aminoethylphosphonate was also present on the third mannose residue distal to glucosamine, partially replacing the ethanolamine phosphate. The β-eliminated reduced oligosaccharide chains showed that two novel classes of O-linked N-acetylglucosamine oligosaccharide were present. The first series had the structures Galpβ1-3GlcNAc-ol; Galpβ1-6(Galpβ1-3)GlcNAc-ol; and Galpβ1-2Galpβ1-6(Galpβ1-3)GlcNAc-ol, whereas the other series had a 1-4 linkage to N-acetylglucosaminitol and had structures Galpβ1-4GlcNAc-ol, Galpβ1-6(Galpβ1-4)GlcNAc-ol, and Galpβ1-2Galpβ1-6(Galpβ1-4)GlcNAc-ol. We have also investigated the kinetics of in vitro sialylation of these O-linked oligosaccharides by the T. cruzi trans-sialidase and have shown that incorporation of one molecule of sialic acid hinders entry of a second molecule when two potential acceptor sites are present." @default.
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• W2078382249 date "1995-03-01" @default.
• W2078382249 modified "2023-10-18" @default.
• W2078382249 title "Structural Characterization of the Major Glycosylphosphatidylinositol Membrane-anchored Glycoprotein from Epimastigote Forms of Trypanosoma cruzi Y-strain" @default.
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• W2078382249 doi "https://doi.org/10.1074/jbc.270.13.7241" @default.
• W2078382249 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/7706263" @default.
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