Phospholipase C from Bacillus cereus and its use in studies of tissue thromboplastin.

Phospholipase C from Bacillus cereus and its use in studies of tissue thromboplastin.
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来自蜡样芽孢杆菌的磷脂酶 C 及其在组织凝血活酶研究中的应用。

DOI:
10.1111/j.1432-1033.1972.tb01832.x
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发表时间:
1972
期刊:
European journal of biochemistry
影响因子:
--
通讯作者:
A. Berre
A. Berre
中科院分区:
--
文献类型:
--
作者:
A. Otnaess;H. Prydz;E. Bjørklid;A. Berre

文献摘要

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本文介绍了一种简化的蜡状芽孢杆菌磷脂酶C的纯化方法。该酶在圆盘电泳法、十二烷基硫酸盐-聚丙烯酰胺凝胶电泳法和分析超速离心法中均一。该酶的相对分子质量为23000,等电点为6.5,由一个亚基组成。二价金属离子是必需的,锌离子的活性最强。当磷脂酶C破坏组织凝血活酶时,组织凝血活酶对凝血因子VII的激活是可逆的。
A simplified method for the purification of phospholipase C from Bacillus cereus is described. The enzyme is homogeneous in disc electrophoresis and in dodecylsulphate-polyacrylamide gel electrophoresis as well as in the analytical ultracentrifuge. The enzyme had a molecular weight of 23000, pI= 6.5 and consisted of one subunit. A divalent metal ion was necessary, Zn2+ was the most active. The activation of factor VII by tissue thromboplastin was reversible when tissue thromboplastin was destroyed by phospholipase C.