1 results match your criteria: "University of Shizuoka. hidari@u-shizuoka-ken.ac.jp[Affiliation]"
Purification and characterization of a soluble recombinant human ST6Gal I functionally expressed in Escherichia coli.
Glycoconj J
February 2005
Department of Biochemistry, School of Pharmaceutical Sciences, Core Research for Evolutional Science and Technology (CREST), Japan Science and Technology Corporation, University of Shizuoka.
A soluble and active form of recombinant human ST6Gal I was expressed in Escherichia coli. The gene encoding the soluble form of ST6Gal I lacking the membrane and cytosolic regions was introduced into a bacterial expression vector, pMAL-p2X, fused in frame with a maltose-binding protein (MBP) tag. Low-temperature cultivation at 13 degrees C during IPTG-induction significantly improved both solubility and MBP-tagging of the recombinant enzyme expressed in bacteria.
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