海産ラビリンチュラ分離株00-Bat-05からのロイシンアミノペプチダーゼの精製と酵素学的性状
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- Md. Iftekharul Wahid
- The United Graduate School of Agricultural Sciences, Kagoshima University
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- Yoshikawa Takeshi
- Laboratory of Microbiology, Faculty of Fisheries, Kagoshima University
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- Sakata Taizo
- Laboratory of Microbiology, Faculty of Fisheries, Kagoshima University
書誌事項
- タイトル別名
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- Purification and Characterization of Leucine Aminopeptidase from Marine Labyrinthulid Strain 00-Bat-05
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抄録
Leucine aminopeptidase (LAP) from marine labyrinthulid strain 00-Bat-05 cells were purified and characterized by enzymological properties. The optimum temperature and pH of LAP from strain 00-Bat-05 was 37°C and pH 8.0, respectively. The thermostability of the enzyme was indicated by remaining 80% of maximum activity after heat treatment at 60°C for 10 min. The enzyme were inactivated by p-chloromercuribenzoic acid (PCMB), 1,10-phenanthroline, bestatin and sodium dodecyl sulphate (SDS), suggesting that it is SH-aminopeptidase. The enzyme activity of LAP was stimulated by Co2+ and inhibited by Zn2+. LAP of 00-Bat-05 had a high specificity for L-leucine-p-nitroanilide among p-nitroanilide derivatives of L-amino acids tested.
収録刊行物
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- 水産増殖
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水産増殖 56 (1), 1-8, 2008
日本水産増殖学会
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詳細情報 詳細情報について
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- CRID
- 1390001204716290304
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- NII論文ID
- 10026138894
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- NII書誌ID
- AN00124667
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- ISSN
- 21850194
- 03714217
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- NDL書誌ID
- 9427299
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- IRDB
- NDL
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可