『徳島大学 教育・研究者情報データベース (EDB)』---[学外] /
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種別 (必須): 学術論文 (審査論文) [継承]
言語 (必須): 英語 [継承]
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審査 (推奨):
カテゴリ (推奨):
共著種別 (推奨):
学究種別 (推奨):
組織 (推奨): 1.徳島大学.工学部.生物工学科.生物反応工学講座 [継承]
著者 (必須): 1.郷田 秀一郎 ([長崎大学])
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2. (英) Takano Kazufumi (日) (読)
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3. (英) Yamagata Yuriko (日) (読)
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4. (英) Katakura Yoshio (日) (読)
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5. (英) Yutani Katsuhide (日) (読)
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題名 (必須): (英) Effect of extra N-terminal residues on the stability and folding of human lysozyme expressed in Pichia pastoris  (日)    [継承]
副題 (任意):
要約 (任意): (英) A human lysozyme expression system by Pichia pastoris was constructed with the expression vector of pPIC9, which contains the alpha-factor signal peptide known for high secretion efficiency. P. pastoris expressed the human lysozyme at about 300 mg/l broth, but four extra residues (Glu(-4)-Ala(-3)-Glu(-2)-Ala(-1)-) were added at the N-terminus of the expressed protein (EAEA-lysozyme). To determine the effect of the four extra residues on the stability, structures and folding of the protein, calorimetry, X-ray crystal analysis and GuHCl denaturation experiments were performed. The calorimetric studies showed that the EAEA-lysozyme was destabilized by 9.6 kJ/mol at pH 2.7 compared with the wild-type protein, mainly caused by the substantial decrease in the enthalpy change (DeltaH). On the basis of structural information on the EAEA-lysozyme, thermodynamic analyses show that (1) the addition of the four residues slightly affected the conformation in other parts far from the N-terminus, (2) the large decrease in the enthalpy change due to the conformational changes would be almost compensated by the decrease in the entropy change and (3) the decrease in the Gibbs energy change between the EAEA and wild-type human lysozymes could be explained by the summation of each Gibbs energy change contributing to the stabilizing factors concerning the extra residues.  (日)    [継承]
キーワード (推奨): 1. (英) Calorimetry, Differential Scanning (日) (読) [継承]
2.X線結晶学 (X-ray crystallography) [継承]
3. (英) Enzyme Stability (日) (読) [継承]
4. (英) Guanidine (日) (読) [継承]
5. (英) Humans (日) (読) [継承]
6. (英) Kinetics (日) (読) [継承]
7. (英) Muramidase (日) (読) [継承]
8. (英) Peptide Fragments (日) (読) [継承]
9. (英) Pichia (日) (読) [継承]
10. (英) Protein Conformation (日) (読) [継承]
11. (英) Protein Denaturation (日) (読) [継承]
12. (英) Protein Folding (日) (読) [継承]
13. (英) Recombinant Fusion Proteins (日) (読) [継承]
14.熱力学 (thermodynamics) [継承]
発行所 (推奨):
誌名 (必須): Protein Engineering ([Oxford University Press])
(pISSN: 0269-2139, eISSN: 1460-213X)

ISSN (任意): 0269-2139
ISSN: 0269-2139 (pISSN: 0269-2139, eISSN: 1460-213X)
Title: Protein engineering
Title(ISO): Protein Eng
Publisher: Oxford University Press
 (NLM Catalog  (Scopus  (CrossRef (Scopus information is found. [need login])
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(必須): 13 [継承]
(必須): 4 [継承]
(必須): 299 307 [継承]
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年月日 (必須): 西暦 2000年 4月 1日 (平成 12年 4月 1日) [継承]
URL (任意):
DOI (任意): 10.1093/protein/13.4.299    (→Scopusで検索) [継承]
PMID (任意): 10810162    (→Scopusで検索) [継承]
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備考 (任意): 1.(英) Article.Affiliation: Institute for Protein Research, Osaka University, Yamadaoka, Suita, Osaka 565-0871, Japan.  (日)    [継承]
2.(英) Article.PublicationTypeList.PublicationType: Journal Article  (日)    [継承]
3.(英) Article.PublicationTypeList.PublicationType: Research Support, Non-U.S. Gov't  (日)    [継承]

標準的な表示

和文冊子 ● Shuichiro Goda, Kazufumi Takano, Yuriko Yamagata, Yoshio Katakura and Katsuhide Yutani : Effect of extra N-terminal residues on the stability and folding of human lysozyme expressed in Pichia pastoris, Protein Engineering, Vol.13, No.4, 299-307, 2000.
欧文冊子 ● Shuichiro Goda, Kazufumi Takano, Yuriko Yamagata, Yoshio Katakura and Katsuhide Yutani : Effect of extra N-terminal residues on the stability and folding of human lysozyme expressed in Pichia pastoris, Protein Engineering, Vol.13, No.4, 299-307, 2000.

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