PMID: 8947472Nov 15, 1996Paper

Interaction of plant lipids with 14 kDa phospholipase A2 enzymes

The Biochemical Journal
Bannikuppe S VishwanathBrigitte M Frey

Abstract

Several structurally related plant lipids were isolated and their effect was assessed on the enzyme activity of group I (pancreatic and Naja mocambique venom) and group II (Crotalus atrox venom) phospholipase A2 (PLA2) enzymes, with labelled Escherichia coli as an enzyme substrate. The neutral monogalactosyldiacylglycerol (MGDG) and negatively charged diacylglyceryl alpha-D-glucuronide (DGGA) did not influence the enzyme activity of either group. Digalactosyldiacylglycerol (DGDG), another uncharged glycolipid, inhibited PLA2 activity in a dose-dependent manner to 60-70% of the control. Sulphoquinovosyldiacylglycerol (SQDG), which is also anionic, activated both groups of PLA2 enzyme. A similar activation was observed with the zwitterionic diacylglyceryl-O-(N,N,N-trimethylhomoserine) (DGTS) and diacylglyceryl-O-(hydroxymethyl)(N,N, N-trimethyl)-beta-alanine (DGTA). DGDG, SQDG and DGTS are dispersed homogeneously with low critical micelle concentrations (CMCs). The hydrodynamic radius of neutral DGDG is an order of magnitude larger than the charged lipids SQDG and DGTS. The inhibition of pig pancreatic PLA2 by DGDG was dependent on substrate concentration. The intrinsic fluorescence spectra of the enzyme was not changed in the pr...Continue Reading

Citations

Oct 3, 2006·Life Sciences·Noor Mohamed JameelBannikuppe S Vishwanath
Oct 29, 2005·European Journal of Pharmacology·Annalisa BrunoDaniela Corda
Jan 1, 2004·The Journal of Biological Chemistry·Osamu TohyamaYo-ichi Nabeshima
Feb 7, 2003·Nature·Jonathan Knight
Sep 18, 2010·The Journal of Medical Investigation : JMI·Asuka ShiotaEiji Takeda
Mar 5, 2011·Progress in Lipid Research·Mie Shimojima

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