[83] Phospholipase C from Bacillus cereus: EC 3.1.4.3 phosphatidylcholine cholinephosphohydrolase
[83] Phospholipase C from Bacillus cereus: EC 3.1.4.3 phosphatidylcholine cholinephosphohydrolase
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[83] 来自蜡状芽孢杆菌的磷脂酶 C：EC 3.1.4.3 磷脂酰胆碱磷酸胆碱水解酶
DOI：
10.1016/0076-6879(81)71085-1
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发表时间：
1981
影响因子：
--
通讯作者：
C. Little
中科院分区：
文献类型：
--
作者：
C. Little
磷脂酶C（磷脂酰胆碱胆碱磷酸水解酶，EC 3.1。4.3)是一种广泛用于膜和磷脂研究的细菌酶。对于此类研究，需要尽可能高的纯度。蜡样芽孢杆菌和产气荚膜梭菌酶都已使用常规技术纯化至表观均一性[1 -3]。然而，使用磷脂酶C高产菌株B.蜡状芽孢杆菌[4]，使用所述纯化方案[2]（C. Little和AB Otnaess，未发表的观察）。C7。产气荚膜杆菌酶也已经通过包括琼脂糖连接的蛋黄脂蛋白上的亲和层析的方法纯化[51]，并且我们已经将该技术应用于B的纯化。蜡状酶本文提出的纯化方案比以前发表的方法更简单、更方便，并且得到更高的酶产率。
Phospholipase C (phosphatidylcholine cholinephosphohydrolase, EC 3.1. 4.3) is a bacterial enzyme widely used in membrane and phospholipid studies. For such studies the highest possible degree of purity is required. Both the Bacillus cereus and the Clostridium perfringens enzymes have been purified to apparent homogeneity using conventional techniques [l-3]. However, using a phospholipase C-hyperproducing strain of B. cereus [4], homogeneous preparations of enzyme were not consistently obtained using the purification scheme described [2](C. Little and AB Otnaess, unpublished observation). The C7. perfringens enzyme has also been purified by a method involving affinity chromatography on agarose-linked egg yolk lipoprotein [51 and we have applied this technique to the purification of the B. cereus enzyme. The purification scheme here presented is simpler and more convenient and gives higher yields of enzyme than do the previously published methods.