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PubMed · 2758074

[Study of phospholipase A2 specificity in substrate-containing structures having different supramolecular organization].

A M Akhrem·T A Shumilina·N M Litvinko·O I Linnik·M A Kisel'
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Abstract

The specificity of snake venom phospholipase A2(PLA2) towards a number of phospholipid (PL) substrates, e. g., phosphatidylcholine (PC), phosphatidylglycerol (PG), phosphatidylethanolamine (PE) and phosphatidylinositol (PI) organized in Triton X-100 mixed micelles, liposomes and proteoliposomes was studied. PC was shown to be more rapidly hydrolyzed in micelles. For other PLs, the rate of hydrolysis decreased in the following sequence: PC greater than PI greater than PE greater than PG. The incorporation into micelles of a non-hydrolyzable by PLA2 sphinogomyelin which, similar to PC, has a choline group, resulted in an increase of PLA2 specificity towards PL that are known to be devoid of this group: PE greater than PI greater than PG greater than PC. Quite a different picture was observed in bilayer liposomal structures: PI congruent to PE greater than PC greater than PG. The incorporation of cytochrome P-450 into liposomes caused the acceleration of PE and PG hydrolysis. The course of the PLA2-catalyzed hydrolysis in model membrane structures seems to be governed primarily by the supramolecular organization and localization of the substrate in the bilayer, but not by its chemical structure.

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AnimalsElapid VenomsHydrolysisMacromolecular SubstancesMicroscopy, ElectronPhospholipasesPhospholipases APhospholipases A2PhospholipidsSubstrate SpecificityJournal Article

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A M Akhrem, T A Shumilina, N M Litvinko, O I Linnik, M A Kisel'. 1989. [Study of phospholipase A2 specificity in substrate-containing structures having different supramolecular organization].. https://pubmed.ncbi.nlm.nih.gov/2758074/

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