Recombinant expression and characterization of N-acetylglucosaminyltransferase I derived from Nicotiana tabacum(PLANT BIOTECHNOLOGY)

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概要

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• The C-terminal catalytic domain of tobacco N-acetylglucosaminyltransferase I fused to maltose-binding protein was produced in Escherichia coli as a soluble form with significant activity. The protein was affinity-purified using amylose resin, and its enzymatic properties were investigated, including its divalent cation requirements, optimal temperature. optimal pH, and substrate specificity.

著者

• Dohi Koji

  International Center for Biotechnology, Osaka University

• Isoyama-Tanaka Junko

  International Center for Biotechnology, Osaka University

• Tokuda Toru

  International Center for Biotechnology, Osaka University

• Fujiyama Kazuhito

  International Center for Biotechnology, Osaka University

• Fujiyama Kazuhito

  International Center For Biotechnology Osaka Univ.

• Fujiyama Kazuhito

  International Center For Biotechnology Osaka University

• Dohi Koji

  International Center For Biotechnology Osaka University

• Tokuda Toru

  International Center For Biotechnology Osaka University

• Fujiyama Kazuhito

  The International Center For Biotechnology Osaka Univ. 2-1 Yamada-oka Suita-shi Osaka 565-0871 Jpn

• Isoyama-tanaka Junko

  International Center For Biotechnology Osaka University

• Fujiyama Kazuhito

  The International Center For Biotechnology Osaka Univ. 2-1 Yamada-oka Suita Osaka 565-0871 Jpn

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