人胎盘碱性磷酸酶对磷脂酸的水解作用。

Hydrolysis of phosphatidate by human placental alkaline phosphatase.

作者信息

Sumikawa K, Saeki K, Okochi T, Adachi K, Nishimura H

出版信息

Clin Chim Acta. 1987 Aug 31;167(3):321-8. doi: 10.1016/0009-8981(87)90352-4.

Abstract

Highly purified alkaline phosphatase of human placenta catalyzed the hydrolysis of phosphatidate with quantitative formation of almost stoichiometric amounts of diglyceride and inorganic phosphate. In the presence of sodium deoxycholate, the activity was maximal at pH 8.8. The activity was strongly inhibited by L-phenylalanine but scarcely affected by NaF. These results show that alkaline phosphatase hydrolyzes phosphatidate under different conditions from those for activity of phosphatidate phosphohydrolase.

摘要

高度纯化的人胎盘碱性磷酸酶催化磷脂酸水解，定量生成几乎化学计量的甘油二酯和无机磷酸。在脱氧胆酸钠存在下，该酶在pH 8.8时活性最高。其活性受到L-苯丙氨酸的强烈抑制，但几乎不受氟化钠的影响。这些结果表明，碱性磷酸酶水解磷脂酸的条件与磷脂酸磷酸水解酶的活性条件不同。