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引用次数: 0
摘要
金黄色葡萄球菌的脂肪酶和磷脂酶C可以在Sephacryl S 200上通过凝胶过滤分离出来(图1a, b),在相同的条件下通过再过滤完全分离。等电聚焦在pH 8.6和9.5时脂肪酶和pH 7.4时磷脂酶C的酶活性最大(图2)。薄层色谱显示,金黄色葡萄球菌和蜡样芽孢杆菌的磷脂酶C制剂在卵磷脂琼脂中的反应产物相同(表1)。
[Lipase and phospholipase from Staphylococcus aureus of different origin. II. Purification and characterization (author's transl)].
Lipase and phospholipase C from Staphylococcus aureus could be isolated by gel filtration on Sephacryl S 200 (Fig. 1a, b) and completely separated by refiltration under the same conditions. Isoelectric focusing gave maximal enzyme-activities for lipase at pH 8.6 and 9.5 and for phospholipase C at pH 7.4 (Fig. 2). Thin-layer chromatography revealed that the reaction products in lecithin agar of the phospholipase C-preparations from S. aureus and Bacillus cereus were identical (Table 1).