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

机译:通过激活长链阴离子产生的磷脂酶D的最佳pH值发生变化

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p1. 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 ζ-potentials (electrophoretic mobilities)./p
机译:> 1。磷脂酶D(磷脂酰胆碱磷脂酰水解酶,EC 3.1.4.4)对超声处理的磷脂酰胆碱或被醚活化的大磷脂酰胆碱颗粒的活性在pH5附近最大,而在pH6以上几乎没有活性。 2.当通过向大的磷脂酰胆碱颗粒中添加磷脂酸来活化酶时,无论添加的活化剂的量如何,最适pH均移至pH6·5。 3.当用低浓度的十二烷基硫酸盐活化该酶时,最适pH为5·5,在pH6以上几乎没有活性。随着十二烷基硫酸盐浓度的增加,pH活性曲线向上移至最适pH 6·5-6·6,其变化幅度取决于水解程度。 4. pH活性曲线的变化不能与通过测量其ζ电位(电泳迁移率)而计算得出的底物颗粒的“表面pH”变化相关。

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