Partial Purification and Some Properties of a Phospholipase C from<i>Pseudomonas</i>sp. Strain KS3.2
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- SUGIMORI Daisuke
- Department of Chemistry and Biology Engineering, Fukui National College of Technology
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- NAKAMURA Masatoshi
- Department of Chemistry and Biology Engineering, Fukui National College of Technology
書誌事項
- タイトル別名
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- Partial Purification and Some Properties of a Phospholipase C from Pseudomonas sp. Strain KS3.2
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An extracellular phospholipase C was partially purified from Pseudomonas sp. strain KS3.2. The enzyme was composed of an approximately 18-kDa peptide. Maximal enzyme activity was found at pH 7.2 and 50 °C. The enzyme retained activity between pH 8 and 9, and 50% activity at about 52 °C for 30 min. The enzyme sample showed the highest activity on phosphatidylcholine and low activity toward other phospholipids.
収録刊行物
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- Bioscience, Biotechnology, and Biochemistry
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Bioscience, Biotechnology, and Biochemistry 70 (2), 535-537, 2006
公益社団法人 日本農芸化学会
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詳細情報 詳細情報について
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- CRID
- 1390001206475786112
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- NII論文ID
- 10018534703
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- NII書誌ID
- AA10824164
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- ISSN
- 13476947
- 09168451
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- NDL書誌ID
- 7833729
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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
- NDL
- Crossref
- CiNii Articles
- KAKEN
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- 使用不可