Efficient Production of Recombinant Human Pleiotrophin in Yeast, Pichia pastoris(Microbiology & Fermentation Technology)
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概要
- 論文の詳細を見る
Approximately 260 mg/l of authentic recombinant human pleiotrophin (rhPTN) was expressed into the medium of high-cell density fermentation using a Pichia pastoris protein expression system. The preprosequence of yeast α-mating factor was used successfully. The recombinant hPTN was efficiently recovered from the medium by expanded bed adsorption, and purified using successive column chromatography steps. In the purified rhPTN preparation, modified rhPTN were scarcely detected. Circular dichroism measurement of the purified PTN showed the presence of the characteristic β-structures in the protein.
- 社団法人日本農芸化学会の論文
- 2003-10-23
著者
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Asami Yukio
Meiji Institute Of Health Science Meiji Milk Products Co. Ltd.
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Asami Yukio
Meiji Cell Technology Center Meiji Milk Products Co. Ltd.
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MURASUGI AKIRA
Meiji Cell Technology Center, Meiji Milk Products Co. Ltd.
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Murasugi Akira
Meiji Institute Of Health Science Meiji Milk Products Co. Ltd.
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Murasugi Akira
Meiji Cell Technology Center Meiji Milk Products Co. Ltd.
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KIDO Isao
Meiji Cell Technology Center, Meiji Milk Products Co., Ltd.
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KUMAI Hideshi
Meiji Cell Technology Center, Meiji Milk Products Co., Ltd.
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Kido Isao
Meiji Cell Technology Center Meiji Milk Products Co. Ltd.
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Kumai Hideshi
Meiji Cell Technology Center Meiji Milk Products Co. Ltd.
関連論文
- Production of Recombinant Human Midkine in Yeast, Pichia pastoris
- Comparison of Three Signals for Secretory Expression of Recombinant Human Midkine in Pichia pastoris(Microbiology & Fermentation Technology)
- Efficient Production of Recombinant Human Pleiotrophin in Yeast, Pichia pastoris(Microbiology & Fermentation Technology)
- Characterization of Partially Truncated Human Midkine Expressed in Pichia pastoris(Microbiology & Fermentation Technology)
- An Approach to the Removal of Yeast Specific O-Linked Oligo-Mannoses from Human Midkine Expressed in Pichia pastoris Using Site-Specific Mutagenesis