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Phospholipase C from Bacillus cereus and Its Use in Studies of Tissue Thromboplastin
Author(s) -
Otnæss AnneBrit,
Prydz Hans,
Bjørklid Eirik,
Berre Åse
Publication year - 1972
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1972.tb01832.x
Subject(s) - bacillus cereus , chemistry , thromboplastin , biochemistry , ultracentrifuge , enzyme , polyacrylamide gel electrophoresis , chromatography , lysozyme , gel electrophoresis , coagulation , biology , genetics , bacteria , psychology , psychiatry
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, Zn 2+ was the most active. The activation of factor VII by tissue thromboplastin was reversible when tissue thromboplastin was destroyed by phospholipase C.

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