Expression of a mammalian α2,6-sialyltransferase gene in Pichia pastoris

被引：7

作者：

Chotigeat, W ^{[1
]}

Chayanunnukul, W ^{[1
]}

Phongdara, A ^{[1
]}

机构：

[1] Prince Songkla Univ, Fac Sci, Dept Biochem, Songkhla 90112, Thailand

来源：

JOURNAL OF BIOTECHNOLOGY | 2000年 / 81卷 / 01期

关键词：

Pichia pastoris; sialic acid; alpha 2,6-sialyltransferase; glycoproteins; oligosaccharide;

D O I：

10.1016/S0168-1656(00)00268-6

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

Terminal sialic acid on oligosaccharides of glycoproteins shows several biological functions of the glycoproteins. The yeast Pichia pastor is normally does not contain sialic acid on the oligosaccharides of glycoproteins. A sialyltransferase (ST) gene was transfected into P. pastoris to assess the possibility of using yeast cells as a host to produce sialoglycoproteins. The expression vectors pPIC3.5 and pPIC9 were used as carriers. The recombinant P. pastoris harbouring ST-pPIC3.5 and ST-pPIC9 had sialyltransferase activity of 1.1 and 10.2 mU l(-1) respectively. The ability of the recombinant ST-pPIC3.5 and ST-pPIC9 to transfer the fluoresceinyl-NeuAc into the cell glycoproteins was 36.9 and 20.9 pmol mg (-1) protein respectively. (C) 2000 Elsevier Science B.V. All rights reserved.

引用

页码：55 / 61

页数：7

共 21 条

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