Renaturation of Lysozyme with a Protein Disulfide Isomerase Chaperone Results in Enzyme Super Activity(BIOCHEMICAL ENGINEERING)
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概要
- 論文の詳細を見る
When the oxidative refolding of lysozyme (Lyzm) was carried out in the presence of protein disulfide isomerase (PDI) an increased refolding rate and a recovered activity exceeding 100% were reproducibly observed. The origin of this excess activity was investigated by HPLC, SDS-PAGE, and mass spectrometry and assessed using an assay for Lyzm activity. The refolding of Lyzm was achieved through the formation of PDI-Lyzm intermediates and the excess activity was derived from the nascent lysozyme released from these complexes. The released lysozyme exhibited a higher molecular activity than observed for the native protein.
- 社団法人日本生物工学会の論文
- 2008-11-25
著者
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Asami Osamu
Toyota Central Research & Development Labs
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Ohshima Yuji
Department Of Biomolecular Science Faculty Of Engineering Gifu University
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NOHARA DAISUKE
Department of Chemical Reaction Engineering, Faculty of Pharmaceutical Sciences, Nagoya City Univers
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Takezawa Aya
Department of Biomolecular Science, Faculty of Engineering, Gifu University
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Sudo Tomoya
Department of Biomolecular Science, Faculty of Engineering, Gifu University
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Sudo Tomoya
Department Of Biomolecular Science Faculty Of Engineering Gifu University
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Takezawa Aya
Department Of Biomolecular Science Faculty Of Engineering Gifu University
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Nohara Daisuke
Department Of Biomolecular Science Faculty Of Engineering Gifu University
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Asami Osamu
Toyota Central Research & Development Labs., Inc.
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