High-level Expression of Maize C_4-type Phosphoenolpyruvate Carboxylase in Escherichia coli and Its Rapid Purification

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概要

• 論文の詳細を見る

• Maize C_4-type phosphoenolpyruvate carboxylase (PEPC) was expressed in E. coli with the pET32 system. The expressed fusion PEPC was active and its amount comprised more than 10% of total soluble protein. The specific activity inbreased by about 45-fold, compared with our previous system [S. Yanagisawa and K. Izui, Agric. Biol. Chem., 54, 241-243 (1990)]. The fusion PEPC was rapidly purified with His bind metal chelation resin, showing a single band on SDS-PAGE. Moreover, the tag domain fused at the N-terminus did not have any effect on catalytic and regulatory properties of PEPC.

• 社団法人日本農芸化学会の論文
• 1997-03-23

著者

• 泉井 桂

  近畿大学生物理工学部生物工学科

• Izui Katsura

  Laboratory Of Plant Physiology Graduate School Of Biostudies Kyoto University

• Izui Katsura

  Laboratory Of Plant Physiology Division Of Applied Biosciences Graduate School Of Agriculture Kyoto

• HATA Shingo

  Laboratory of Plant Physiology, Graduate School of Agriculture, Kyoto University

• Dong Long-Ying

  Laboratory of Plant Physiology, Graduate School of Agriculture, Kyoto University

• DONG Long-Ying

  Div. Appl. Biosci., Grad. Sch. Agr., Kyoto Univ.

• Ishiyama Keiki

  Graduate School Of Agricultural Science Tohoku University

• Ishiyama Keiki

  Riken Plant Science Center

• Dong Long-ying

  Div. Appl. Biosci. Grad. Sch. Agr. Kyoto Univ.

• Hata Shingo

  Laboratory Of Crop Science Graduate School Of Bioagricultural Sciences Nagoya University

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