Production and characterization of active soluble human beta 1,4-galactosyltransferase in Escherichia coli as a useful catalyst in synthesis of the Gal beta 1 arrow right 4 GlcNAc linkage

Production and characterization of active soluble human beta 1,4-galactosyltransferase in Escherichia coli as a useful catalyst in synthesis of the Gal beta 1 arrow right 4 GlcNAc linkage

An active and soluble human beta 1,4-galactosyltransferase ( beta -GT) was produced in Escherichia coli using a maltose-binding protein fusion system. The purified recombinant beta -GT has a K sub(m) value of 0.035 mM for UDP-galactose and a V sub(max) of 643 x 10 super(3) nmol/mg/h. The enzyme cata...

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Veröffentlicht in:Journal of bioscience and bioengineering 2001-01, Vol.91 (1), p.85-87
Hauptverfasser: Shibatani, Shigeo, Fujiyama, Kazuhito, Nishiguchi, Susumu, Seki, Tatsuji, Maekawa, Yoshihiko
Format: Artikel
Sprache:eng
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Zusammenfassung:An active and soluble human beta 1,4-galactosyltransferase ( beta -GT) was produced in Escherichia coli using a maltose-binding protein fusion system. The purified recombinant beta -GT has a K sub(m) value of 0.035 mM for UDP-galactose and a V sub(max) of 643 x 10 super(3) nmol/mg/h. The enzyme catalyzes the transfer of galactose from UDP-galactose to N-linked oligosaccharides. The properties of the purified enzyme were identical to those of bovine milk beta -GT.
ISSN:1389-1723