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Expression of soluble active human beta 1,4 galactosyltransferase in Saccharomyces cerevisiae.

Abstract：

:Sequences coding for the cytoplasmic and transmembrane domains were removed from the cDNA of the human Golgi resident membrane protein beta 1,4 galactosyltransferase (gal-T). The remaining sequences coding for the stem and catalytical domains of this glycosyltransferase were fused to sequences coding for the yeast invertase signal sequence. The hybrid was inserted together with a constitutive yeast promoter and a terminator into a E. coli/yeast shuttle vector. Saccharomyces cerevisiae strain BT150 transformed with this new expression vector expressed enzymically active soluble enzyme, whereas no activity was detectable in mock-transformed yeasts. The enzyme product was identified by HPLC analysis and shown to correspond to the expected product N-acetyllactosamine.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Kleene R,Krezdorn CH,Watzele G,Meyhack B,Herrmann GF,Wandrey C,Berger EG

doi

10.1006/bbrc.1994.1683

subject

Has Abstract

pub_date

1994-05-30 00:00:00

pages

160-7

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(84)71683-4

journal_volume

201

pub_type

杂志文章

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