Expression of a mammalian alpha 2,6-sialyltransferase gene in Pichia pastoris.

Abstract:

:Terminal sialic acid on oligosaccharides of glycoproteins shows several biological functions of the glycoproteins. The yeast Pichia pastoris 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.

journal_name

J Biotechnol

journal_title

Journal of biotechnology

authors

Chotigeat W,Chayanunnukul W,Phongdara A

doi

10.1016/s0168-1656(00)00268-6

subject

Has Abstract

pub_date

2000-07-28 00:00:00

pages

55-61

issue

1

eissn

0168-1656

issn

1873-4863

pii

S0168-1656(00)00268-6

journal_volume

81

pub_type

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