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
Lee,YC
中科院分区:
生物学4区
文献类型:
--
作者:
Takahashi,N;Lee,KB;Nakagawa,H;Tsukamoto,Y;Kawamura,Y;Li,YT;Lee,YC

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相似文献

使用来自克氏锥虫的 α-(2,3)-特异性反式唾液酸酶,从具有末端 Gal 残基的吡啶基-2-氨基寡糖通过酶法制备 α-(2,3)-唾液酸化二触角和三触角寡糖(Lee, K. B. 和 Lee, Y. C. (1994) Anal. Biochem. 216, 358-364)。从人纤维蛋白原中性和α-(2,6)-单唾液酸化二触角寡糖的吡啶基-2-氨基衍生物中,获得了5种不同的唾液酸二触角寡糖。从来自胎球蛋白的两种不同的脱唾液酸三触角寡糖中,获得了 35 种唾液酸寡糖。转唾液酸酶有效且无差别地将唾液酸转移至底物上不同位置的不同半乳糖基残基。由于起始材料是已确定结构的中性寡糖,并且唯一的 α-(2,3)-唾液酸残基被添加到非还原性 Gal 末端残基上,因此可以通过使用三维作图技术明确地鉴定这些寡糖的结构(Takahashi, N.、Nakakawa, H.、Fujikawa, K.、Kawamura, Y. 和 Tomiya, N. (1995) Anal. Biochem. 226, 139-146.) 与 β-半乳糖苷酶、β-N-己糖胺酶和唾液酸酶 L 的策略性消化相结合。
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.