Partial Purification and Some Properties of a Phospholipase C from Pseudomonas sp. Strain KS3.2
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概要
- 論文の詳細を見る
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.
- 社団法人 日本農芸化学会の論文
- 2006-02-23
著者
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Nakamura Masatoshi
Department of Pediatric Surgery, Reproductive and Developmental Medicine, Graduate School of Medical
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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 Advanced Systems Control Engineering Graduate School Of Science And Engineering Saga U
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