Dipalmitoyl-phosphatidylcholine/phospholipase D interactions investigated with polarization-modulated infrared reflection absorption spectroscopy

被引：46

作者：

Estrela-Lopis, I ^{[1
]}

Brezesinski, G ^{[1
]}

Möhwald, H ^{[1
]}

机构：

[1] Max Planck Inst Colloids & Interfaces, D-14476 Golm, Germany

来源：

BIOPHYSICAL JOURNAL | 2001年 / 80卷 / 02期

关键词：

D O I：

10.1016/S0006-3495(01)76054-7

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

The hydrolysis of 1,2-dipalmitoylphosphatidylcholine (DPPC) catalyzed by Streptomyces chromofuscus phospholipase D (PLD) has been investigated using monolayer techniques and polarization-modulated infrared absorption reflection spectroscopy. The spectroscopic analysis of the phosphate groups provides a quantitative estimation of the hydrolysis yield. The hydrolysis kinetics was investigated in dependence on the phase state of the lipid monolayer. It was found that PLD exhibits maximum activity in the liquid-expanded phase, whereas PLA, has its activity maximum in the two-phase region, A lag phase was observed in all experiments indicating that small amounts of the hydrolysis product 1,2-dipalmitoylphosphatidic acid (DPPA) are needed for initiating the fast hydrolysis reaction. Higher concentrations of DPPA inhibit the hydrolysis. The critical inhibition concentration of DPPA is a function of the monolayer pressure.

引用

页码：749 / 754

页数：6

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