『徳島大学 教育・研究者情報データベース (EDB)』---[学外] /
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EID=82895EID:82895, Map:0, LastModified:2011年6月23日(木) 11:29:41, Operator:[佐藤 高則], Avail:TRUE, Censor:0, Owner:[佐藤 高則], Read:継承, Write:継承, Delete:継承.
種別 (必須): 国内講演発表 [継承]
言語 (必須): 日本語 [継承]
招待 (推奨):
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カテゴリ (推奨): 研究 [継承]
共著種別 (推奨):
学究種別 (推奨): 学士課程学生による研究報告 [継承]
組織 (推奨): 1.徳島大学.総合科学部.自然システム学科 (1993年4月1日〜) [継承]
著者 (必須): 1. (英) Sugiyama Noriko (日) (読)
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[継承]
2. (英) Kohaku Yuko (日) (読)
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[継承]
3. (英) Kouzai Miho (日) (読)
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4. (英) Yamaguchi Yasuaki (日) (読)
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5.佐藤 高則
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題名 (必須): (英) A drastic decrease in thermostability of Thermus thermophilus Inorganic Pyrophosphatase by substitution of Cysteine 168 to hydrophobic amino acids.  (日)    [継承]
副題 (任意):
要約 (任意): (英) Thermus thermophilus Inorganic pyrophosphatase (Tth PPase) is comprised of homohexamer, and exhibits high thermostability. However, it had not been elucidated that C-terminal region may contribute to its thermostability of Tth PPase. Therefore, we focused on sole cysteine (Cys168) in molecule, and examined the contribution of this Cys residue to the thermostability of Tth PPase by substitution to hydrophobic amino acids. Firstly, we prepared the three Cys168-substituted variants (C168 L, I, and F) by site-directed mutagenesis, followed by examined their enzyme activities and oligomeric structure. In native state, though wild type Tth PPase and all variants maintained the hexameric state, enzyme activity of only C168F was decreased to 58% of the wild type. On the other hand, the thermostabilities of enzyme activity and quaternary structure in all variants were decreased drastically relative to those of the wild type. In particular, C168I variant was dissociated into trimer and monomer after heating even at 65°C, which is appeared to be the most unstable of all variants. Therefore, it was suggested that the microenvironment around Cys168 in Tth PPase must be hydrophilic and less bulky for its thermostability and structural integrity, and C-terminal region of Tth PPase may play a key role in the stability of whole molecule.  (日)    [継承]
キーワード (推奨):
発行所 (推奨): 日本生化学会 [継承]
誌名 (必須): 生化学 ([日本生化学会])
(resolved by 0037-1017)
ISSN: 0037-1017 (pISSN: 0037-1017, eISSN: 2189-0544)
Title: Seikagaku. The Journal of Japanese Biochemical Society
Title(ISO): Seikagaku
Publisher: Nihon Seikagakkai/Japanese Biochemical Society
 (NLM Catalog  (医中誌Web  (Scopus (Scopus information is found. [need login])
(resolved by 2189-0544)
ISSN: 0037-1017 (pISSN: 0037-1017, eISSN: 2189-0544)
Title: Seikagaku. The Journal of Japanese Biochemical Society
Title(ISO): Seikagaku
Publisher: Nihon Seikagakkai/Japanese Biochemical Society
 (NLM Catalog  (医中誌Web  (Scopus (Scopus information is found. [need login])

ISSN (任意):
[継承]
(必須): 76 [継承]
(必須): 8 [継承]
(必須): 809 809 [継承]
都市 (必須): 横浜 (Yokohama/[日本国]) [継承]
年月日 (必須): 西暦 2004年 10月 14日 (平成 16年 10月 14日) [継承]
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標準的な表示

和文冊子 ● Noriko Sugiyama, Yuko Kohaku, Miho Kouzai, Yasuaki Yamaguchi, 佐藤 高則 : A drastic decrease in thermostability of Thermus thermophilus Inorganic Pyrophosphatase by substitution of Cysteine 168 to hydrophobic amino acids., 生化学, Vol.76, No.8, 809, 2004年10月.
欧文冊子 ● Noriko Sugiyama, Yuko Kohaku, Miho Kouzai, Yasuaki Yamaguchi and Takanori Satoh : A drastic decrease in thermostability of Thermus thermophilus Inorganic Pyrophosphatase by substitution of Cysteine 168 to hydrophobic amino acids., Seikagaku, Vol.76, No.8, 809, Oct. 2004.

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