Enzymatic Properties of an Extracellular Phospholipase C Purified from a Marine Streptomycete
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概要
- 論文の詳細を見る
A novel extracellular phospholipase C (PLC) was purified from a marine streptomycete. It had a molecular mass of 28 kDa as estimated by SDS-polyacrylamide gel electrophoresis. Its enzyme activity was optimal at pH 8.0 at 45 °C. The PLC hydrolyzed only phosphatidylcholine. Its activity was enhanced 300% by Na+ (200 mM), suggesting that the purified PLC is a typical marine-type enzyme.
- 社団法人 日本農芸化学会の論文
- 2009-09-23
著者
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Cho Ki
Department Of Electronic Materials Engineering Korea Advanced Institute Of Science And Technology
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Kim Jae-heon
Department Of Microbiology And Institute Of Basic Sciences Dankook University
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Cho Ki
Department Of Marine Biotechnology Anyang University
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MO SangJoon
Department of Chemistry and Nano Science, Ewha Womans University
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Mo Sangjoon
Department Of Chemistry And Nano Science Ewha Womans University
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