Mo SangJoon, Kim Jae-Heon, Cho Ki Woong
Department of Chemistry and Nano Science, Ewha Womans University, Seoul 120-750, Korea.
Biosci Biotechnol Biochem. 2009 Sep;73(9):2136-7. doi: 10.1271/bbb.90323. Epub 2009 Sep 7.
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 degrees Celsius. 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.
从一种海洋链霉菌中纯化出一种新型细胞外磷脂酶C（PLC）。通过SDS-聚丙烯酰胺凝胶电泳估计，其分子量为28 kDa。其酶活性在45摄氏度、pH 8.0时最佳。该PLC仅水解磷脂酰胆碱。Na⁺（200 mM）可使其活性提高300%，这表明纯化的PLC是一种典型的海洋型酶。
