Enzymatic sialylation of N-linked oligosaccharides using an alpha-(2,3)-specific trans-sialidase from Trypanosoma cruzi: structural identification using a three-dimensional elution mapping technique.
Enzymatic sialylation of N-linked oligosaccharides using an alpha-(2,3)-specific trans-sialidase from Trypanosoma cruzi: structural identification using a three-dimensional elution mapping technique.
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使用来自克氏锥虫的 α-(2,3) 特异性转唾液酸酶对 N-连接寡糖进行酶促唾液酸化:使用三维洗脱图谱技术进行结构鉴定。
DOI:
10.1006/abio.1995.1483
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发表时间:
1995
影响因子:
2.9
通讯作者:
Lee,YC
中科院分区:
文献类型:
--
作者:
Takahashi,N;Lee,KB;Nakagawa,H;Tsukamoto,Y;Kawamura,Y;Li,YT;Lee,YC
α-(2,3)-Sialylated biantennary and triantennary oligosaccharides were enzymatically prepared from pyridyl-2-amino-oligosaccharides with terminal Gal residues, using an α-(2,3)-specific trans-sialidase from Trypanosoma cruzi (Lee, K. B., and Lee, Y. C. (1994) Anal. Biochem. 216, 358-364). From the pyridyl-2-amino-derivatives of neutral and α-(2,6)-monosialylated biantennary oligosaccharides from human fibrinogen, 5 different sialyl biantennary oligosaccharides were obtained. From two different asialo-triantennary oligosaccharides from fetuin, 35 sialyl oligosaccharides were obtained. The trans-sialidase transferred sialic acids effectively and indiscriminately to different galactosyl residues in the different positions on the substrates. Since the starting materials are neutral oligosaccharide of established structure, and the only α-(2,3)-sialyl residues are added to the nonreducing Gal terminal residues, the structures of these oligosaccharides could be identified unambiguously by using the three-dimensional mapping technique (Takahashi, N., Nakagawa, H., Fujikawa, K., Kawamura, Y., and Tomiya, N. (1995) Anal. Biochem. 226, 139-146.) in combinations with strategic digestion with β-galactosidase, β-N-hexosaminidase, and sialidase L.