【摘要】 对一种纯化自Bacillus mycoides970发酵上清液的磷脂酶C的部分特性进行了研究。SDS-PAGE检测表明该纯化磷脂酶C由一条多肽链组成,分子量为75.1 kDa。热稳定性实验表明该纯化磷脂酶C对温度敏感,具有热不稳定性。金属离子依赖性检测表明该纯化磷脂酶C属于金属磷脂酶C家族,Ca2+、Mg2+、Zn2+和Ba2+对该磷脂酶C催化活性的发挥必不可少。血平板及卵黄平板检测表明该磷脂酶C没有溶血活性和卵磷脂酶活性。更多还原

【Abstract】 Some properties of phospholipase C(PLC) from Bacillus mycoides 970 are studied in this paper.The PLC is indicated to be a single polypeptide and its molecular mass is estimated to be 75.1 kDa by the SDS-PAGE.The PLC is sensitive to temperature and is heat-labile.The PLC belongs to a group of metallophospholipase C and Zn2+,Ca2+,Mg2+ and Ba2+ are essential for its hydrolyzing activity.The enzyme shows no lecithinase activity on egg yolk agar and no hemolytic activity to human erythrocytes on blood agar.更多还原