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. 2008 Aug 25;59(13):3587–3594. doi: 10.1093/jxb/ern208

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© 2008 The Author(s).

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

This paper is available online free of all access charges (see http://jxb.oxfordjournals.org/open_access.html for further details)

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Fig. 4. — The effect of aristolochic acid (Aris), a low molecular weight PLA₂ inhibitor, on the activity of purified PLA₂β. (A) Light-induced stomatal opening of wild-type Arabidopsis in the presence or absence of 20 μM Aris. (B) Thin layer chromatography (TLC) analysis of the hydrolytic activity of recombinant PLA₂β. Purified PLA₂β was incubated in 100 mM TRIS–HCl (pH 8.0) at 40 °C in the presence or absence of 20 μM Aris for 40 min, and then PLA₂β hydrolytic activity was assayed in the presence of 1-palmitoyl-2-[¹⁴C]palmitoyl-PC. The acyl-hydrolysis activity of the recombinant protein was greatly inhibited by Aris, compared to the solvent controls. Lane 1, substrate only; lanes 2–3, solvent controls (40 μM NaOH); lanes 4–5, 20 μM Aris dissolved in NaOH; lane 6, bee venom low molecular weight secretory PLA₂ was used instead of purified PLA₂β to identify the position of ¹⁴C-palmitic acid in the TLC plate. (C) The results from TLC were quantified using a phosphoimager (n=4).