Abstract
α2,3-Sialylation of the lactosamine type N-glycans with trans-sialidase from Trypanosoma cruzi is reported. Trans-sialidase (160 kDa, pI 5.35–5.65) and its catalytic fragment (70 kDa, pI 6.0–6.3) were isolated from T. сruzi cells and immobilized on ConA-Sepharose. The resulting preparation retained its activity for several months and was repeatedly used for obtaining mono-, di-, tri-, and tetrasialylated 7-amino-4-metylcoumarin-labeled oligosaccharides with various numbers of antennas and for α2,3-sialylation of glycans within glycoproteins and neoglycoconjugates.
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Shiyan, S.D., Zueva, V.S., Nasonov, V.V. et al. Sialylation of N-Carbohydrate Chains of Glycoproteins with Trans-Sialidase from Trypanosoma cruzi . Russian Journal of Bioorganic Chemistry 30, 358–366 (2004). https://doi.org/10.1023/B:RUBI.0000037263.04462.97
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DOI: https://doi.org/10.1023/B:RUBI.0000037263.04462.97