奎宁对韦氏梭菌磷脂酶C的激活作用：对钙离子的绝对需求。
The activation of phospholipase C from Clostridium Welchii by quinine: an absolute requirement for calcium ions.
作者信息
Klein R, Miller N, Kemp P, Laser H
出版信息
Chem Phys Lipids. 1975 Sep;15(1):15-26. doi: 10.1016/0009-3084(75)90027-4.
Quinine activates the hydrolysis of phosphatidyl choline suspensions by phospholipase C (E.C. 3.1.4.3) obtained from Clostridium welchii. Low levels of calcium are an absolute requirement for this activation: Mg2+, Ba2+, Sr2+, and Zn2+ are ineffective. The induction period, or lag phase for this enzyme is dependent upon both calcium concentration and substrate interfacial surface area. At low concentrations (less then 50 muM) calcium ions affect the induction period but not the maximal rate of hydrolysis, whereas guinine predominantly affects the rate of hydrolysis by alterations in the surface charge carried by the substrate.
奎宁可激活由产气荚膜梭菌获得的磷脂酶C（E.C. 3.1.4.3）对磷脂酰胆碱悬浮液的水解作用。这种激活绝对需要低水平的钙：Mg2+、Ba2+、Sr2+和Zn2+无效。该酶的诱导期或延迟期取决于钙浓度和底物界面表面积。在低浓度（低于50μM）时，钙离子影响诱导期，但不影响最大水解速率，而奎宁主要通过改变底物携带的表面电荷来影响水解速率。
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