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由长链阴离子激活产生的磷脂酶D最佳pH值的变化。

A shift in the optimum pH of pospholipase D produced by activating long-chain anions.

作者信息

Quarles R H, Dawson R M

出版信息

Biochem J. 1969 May;112(5):795-9. doi: 10.1042/bj1120795.

Abstract
  1. The activity of phospholipase D (phosphatidylcholine phosphatidohydrolase, EC 3.1.4.4) towards ultrasonically treated phosphatidylcholine or large phosphatidylcholine particles activated with ether was maximal near pH5, and there was little activity above pH6. 2. When the enzyme was activated by the addition of phosphatidic acid to large phosphatidylcholine particles the pH optimum was shifted to pH6.5 irrespective of the amount of activator added. 3. When the enzyme was activated with low concentrations of dodecyl sulphate the pH optimum was 5.5 with little activity above pH6. With higher concentrations of dodecyl sulphate the pH-activity profile was shifted upwards towards a pH optimum of 6.5-6.6, the magnitude of the shift depending on the extent of the hydrolysis. 4. The shifts in the pH-activity profiles cannot be correlated with changes in the ;surface pH' of the substrate particles calculated from the measurement of their zeta-potentials (electrophoretic mobilities).
摘要
  1. 磷脂酶D(磷脂酰胆碱磷脂水解酶,EC 3.1.4.4)对经超声处理的磷脂酰胆碱或用乙醚活化的大磷脂酰胆碱颗粒的活性在pH5附近最大,在pH6以上活性很低。2. 当通过向大磷脂酰胆碱颗粒中添加磷脂酸来激活该酶时,无论添加的激活剂数量如何,最适pH都移至pH6.5。3. 当用低浓度的十二烷基硫酸盐激活该酶时,最适pH为5.5,在pH6以上活性很低。使用较高浓度的十二烷基硫酸盐时,pH-活性曲线向上移动,最适pH为6.5 - 6.6,移动幅度取决于水解程度。4. pH-活性曲线的移动与根据底物颗粒的ζ电位(电泳迁移率)测量计算出的底物颗粒“表面pH”的变化无关。

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