[产气荚膜梭菌磷脂酶C同工酶1的纯化及其性质]
[Purification of phospholipase C isoenzyme 1 from Clostridium perfringens and its properties].
作者信息
Rakhimov M M, Akhmezhanov R A, Sof'ina E Ia, Sagatova F A, Shemanova G F
出版信息
Biokhimiia. 1989 Aug;54(8):1315-24.
A procedure for the purification of isoenzyme I of phospholipase C from Cl. perfringens was developed. The isoenzyme was purified to homogeneity (data from disc electrophoresis) using affinity chromatography on polycephamide and gel filtration through Ultrogel AcA-54, the enzyme yield being 41%. Some properties of the purified isoenzyme I (pH and temperature optima, stability, effect of metal ions and detergents, substrate dependence) were investigated. No significant differences between the properties of the unfractionated enzyme and isoenzyme I were established.
已开发出一种从产气荚膜梭菌中纯化磷脂酶C同工酶I的方法。通过在聚酰胺上进行亲和色谱和使用Ultrogel AcA - 54进行凝胶过滤，将该同工酶纯化至同质（圆盘电泳数据），酶产率为41%。研究了纯化的同工酶I的一些特性（最适pH和温度、稳定性、金属离子和去污剂的影响、底物依赖性）。未发现未分级酶和同工酶I的特性之间存在显著差异。
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