Biochemistry (Moscow)

, Volume 79, Issue 7, pp 687–693 | Cite as

Effect of detergents, trypsin, and bivalent metal ions on interfacial activation and functioning of phospholipase D

  • Sh. R. MadyarovEmail author


The effects of detergents, trypsin, and bivalent metal ions on production of phosphatidic and lysophosphatidic acids by the action of phospholipase D (PLD) on lecithin and lysolecithin were studied. It was found that these reaction products and dodecyl sulfate ions activate PLD, whereas other anionic detergents are less effective. A protective effect of the functioning enzyme against its hydrolytic inactivation by trypsin was found. Bivalent metal ions can be arranged in the following sequence by their ability to activate PLD in the hydrolysis of lecithin and lysolecithin: Ca2+ > Sr2+ > Ba2+ > Mg2+. These results are considered in relation to a proposed mechanism of activation and functioning of PLD with the participation of clusters of phosphatidates and lysophosphatidates. Such Me2+-induced formation of rafts or microdomains from the products of hydrolysis of phospholipids can rationalize not only PLD activation and self-regulation, but also the action of this mechanism on other components and properties of biomembranes. PLD and other lipolytic enzymes can be classified as lateral vector enzymes.

Key words

phospholipase D detergents trypsin metal ions phosphatidates lysophosphatidates activation function regulation biomembranes 





deoxycholic acid


free fatty acid


lysophosphatidic acid






bivalent metal ions


phosphatidic acid






phospholipases A2, C, and D, respectively


sodium dodecyl sulfate


taurocholic acid


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© Pleiades Publishing, Ltd. 2014

Authors and Affiliations

  1. 1.Institute of the Gene Pool of Plants and AnimalsUzbek Academy of SciencesTashkentUzbekistan

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