『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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著者 (必須): 1.増田 かなめ ([徳島大学.大学院医歯薬学研究部.歯学域.口腔科学部門.基礎歯学系.予防歯学]/->個人[三木 かなめ])
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2.吉岡 昌美
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3.日野出 大輔 ([徳島大学.大学院医歯薬学研究部.歯学域.口腔科学部門.口腔保健学系.口腔保健衛生学]/[徳島大学.歯学部.口腔保健学科.口腔保健基礎学講座])
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4.中村 亮 ([徳島大学])
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題名 (必須): (英) Purification and characterization of arginine carboxypeptidase produced by Porphyromonas gingivalis  (日)    [継承]
副題 (任意):
要約 (任意): (英) Arginine carboxypeptidase was isolated from the cytoplasm of Porphyromonas gingivalis 381 and purified by DEAE-Sephacel column chromatography, followed by high-performance liquid chromatography on DEAE-5PW and TSK G2000SW(XL). Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the purified enzyme revealed the presence of three major bands at 42, 33, and 32 kDa with identical N-terminal sequences. By Western blotting analysis and immunoelectron microscopy, the arginine carboxypeptidase was found to be widely distributed in the cytoplasm and on the surface of the outer membrane. The open reading frame corresponding to the N-terminal amino acids of the arginine carboxypeptidase was detected by a search of the sequence of the P. gingivalis W83 genome. This sequence showed homology with mammalian carboxypeptidases (M, N, and E/H) and included a zinc-binding region signature, suggesting that the enzyme is a member of the zinc carboxypeptidase family. The purified enzyme was inhibited by EGTA, o-phenanthroline, DL-2-mercaptomethyl-3-guanidinoethylthiopropanoic acid, and some metal ions, such as Cu(2+), Zn(2+), and Cd(2+). On the other hand, Co(2+) activated the enzyme. The enzyme released arginine and/or lysine from biologically active peptides containing these amino acids at the C terminus but did not cleave substrates when proline was present at the penultimate position. These results indicate that the arginine carboxypeptidase produced by P. gingivalis is an exo type of metallocarboxypeptidase. This enzyme may function to release arginine in collaboration with an arginine aminopeptidase, e.g., Arg-gingipain, to obtain specific amino acids from host tissues during the growth of P. gingivalis.  (日)    [継承]
キーワード (推奨): 1. (英) 3-Mercaptopropionic Acid (日) (読) [継承]
2. (英) Amino Acid Sequence (日) (読) [継承]
3. (英) Base Sequence (日) (読) [継承]
4. (英) Carboxypeptidase B2 (日) (読) [継承]
5. (英) Hydrogen-Ion Concentration (日) (読) [継承]
6. (英) Molecular Sequence Data (日) (読) [継承]
7. (英) Molecular Weight (日) (読) [継承]
8. (英) Porphyromonas gingivalis (日) (読) [継承]
9. (英) Substrate Specificity (日) (読) [継承]
発行所 (推奨):
誌名 (必須): Infection and Immunity ([アメリカ微生物学会])
(pISSN: 0019-9567, eISSN: 1098-5522)

ISSN (任意): 0019-9567
ISSN: 0019-9567 (pISSN: 0019-9567, eISSN: 1098-5522)
Title: Infection and immunity
Title(ISO): Infect. Immun.
Publisher: American Society for Microbiology
 (NLM Catalog  (Scopus  (CrossRef (Scopus information is found. [need login])
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(必須): 70 [継承]
(必須): 4 [継承]
(必須): 1807 1815 [継承]
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年月日 (必須): 西暦 2002年 4月 初日 (平成 14年 4月 初日) [継承]
URL (任意):
DOI (任意): 10.1128/IAI.70.4.1807-1815.2002    (→Scopusで検索) [継承]
PMID (任意): 11895942    (→Scopusで検索) [継承]
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備考 (任意): 1.(英) Article.PublicationTypeList.PublicationType: Journal Article  (日)    [継承]
2.(英) Article.PublicationTypeList.PublicationType: Research Support, Non-U.S. Gov't  (日)    [継承]

標準的な表示

和文冊子 ● Kaname Masuda, Masami Yoshioka, Daisuke Hinode and Ryo Nakamura : Purification and characterization of arginine carboxypeptidase produced by Porphyromonas gingivalis, Infection and Immunity, Vol.70, No.4, 1807-1815, 2002.
欧文冊子 ● Kaname Masuda, Masami Yoshioka, Daisuke Hinode and Ryo Nakamura : Purification and characterization of arginine carboxypeptidase produced by Porphyromonas gingivalis, Infection and Immunity, Vol.70, No.4, 1807-1815, 2002.

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