[Sialylation of N-carbohydrate chains of glycoproteins with immobilized trans-sialidase from Trypanosoma cruzi].
Alpha2,3-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. cruzi cells and immobilized on ConA-Sepharose. The resulting preparation retained activity for several months and was repeatedly used for obtaining mono-, di-, tri-, and tetrasialylated 7-amino-4-metylcoumarine-labeled oligosaccharides with various numbers of antennas and for alpha2,3-sialylation of glycans within glycoproteins and neoglycoconjugates.
Shiian
S D
SD
Zueva
V S
VS
Nasonov
V V
VV
Zhigis
L S
LS
Tsoĭ
N Ts
NTs
Bovin
N B
NB
D000818:Animals; D002850:Chromatography, Gel; D004800:Enzymes, Immobilized; D006023:Glycoproteins / Q000737:chemistry*; D019158:N-Acetylneuraminic Acid / Q000737:chemistry*; D009439:Neuraminidase / Q000737:chemistry* / Q000302:isolation & purification; D011134:Polysaccharides / Q000737:chemistry; D012685:Sepharose / Q000031:analogs & derivatives* / Q000737:chemistry; D014349:Trypanosoma cruzi / Q000201:enzymology*
D004800:Enzymes, Immobilized; D006023:Glycoproteins; D011134:Polysaccharides; C028326:concanavalin A-sepharose; D012685:Sepharose; C069715:trans-sialidase; D009439:Neuraminidase; D019158:N-Acetylneuraminic Acid