Structure of Folding Intermediates at pH 4.0 and Native State of Microbial Transglutaminase(Biochemistry & Molecular Biology)
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概要
- 論文の詳細を見る
Recombinant microbial transglutaminase has been expressed in Escherichia coli as insoluble inclusion bodies. After we searched for refolding conditions, refolding of the protein could be done by first dilution of the unfolded enzyme in a buffer at pH 4.0, and then by titration of the pH from 4.0 to 6.0. CD analysis showed that a burst of secondary structure formation occurred within the dead time of the experiment and accounted for 75% of the signal change in the far UV CD, with little tertiary structure being formed. This burst was followed by slow rearrangement of the secondary structure accompanied by formation of tertiary structure. The secondary and tertiary structures of the final sample at pH 4.0, corresponding to the folding intermediate, were different from these structures at pH 6.0. Once the native structure was obtained, acidification of the native protein to pH 4.0 did not lead to a structure like that of the folding intermediate. Sedimentation velocity analysis showed that the folding intermediate had an expanded structure and contained no other structure species including large aggregates.
- 社団法人日本農芸化学会の論文
- 2003-02-23
著者
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PHILO John
Alliance Protein Laboratories, 3957 Corte Cancion, Thousand Oaks
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ARAKAWA Tsutomu
Alliance Protein Laboratories, 3957 Corte Cancion, Thousand Oaks
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YOKOYAMA Kei-ichi
Central Research Laboratories, Ajinomoto Co. Inc.
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Philo J
Alliance Protein Laboratories
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Philo John
Alliance Protein Laboratories 3957 Corte Cancion Thousand Oaks
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Arakawa T
Alliance Protein Laboratories
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Arakawa Tsutomu
Alliance Protein Lab.
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Ejima Daisuke
Central Research Laboratories Ajinomoto Co. Inc.
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KITA Yoshiko
Alliance Protein Laboratories, 3957 Corte Cancion, Thousand Oaks
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Kita Yoshiko
Alliance Protein Laboratories
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Arakawa T
Allaiance Protein Laboratories
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Yokoyama Kei-ichi
Central Research Laboratories Ajinomoto Co. Inc.
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PHILO John
Alliance Protein Laboratories
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