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. Author manuscript; available in PMC: 2009 Oct 25.
Published in final edited form as: FASEB J. 2007 May 2;21(11):2961–2969. doi: 10.1096/fj.07-8112com

Figure 3.

Figure 3

Pharmacokinetics of plant-produced AChE-RER. A) AChE-RER clearance profile. Groups of 5 mice were injected with either 400 U, 1000 U of plant-produced AChE-RER or an equivalent volume of saline. Plasma samples were collected and assayed for AChE activity in the presence of Iso-OMPA, a selective BChE inhibitor. B) Immunoblot detection of intact circulating AChE-RER. Plasma protein samples from 2 mice injected with 400 U AChE-RER were resolved by SDS-PAGE and subjected to immunoblotting. A 1.3 μg sample of pure plant-derived AChE-RER was resolved alongside for comparison. C) Circulating AChE-RER displays decreased migration in nondenaturing PAGE. Plasma samples from 5 mice injected with 400 U AChE-RER and 2 mice injected with PBS were prepared and subjected to nondenaturing PAGE, followed by staining of catalytically active AChE. Fast migrating AChE-R monomers appeared only after injection of the recombinant enzyme. In panels B, C, purified plant-produced AChE-RER was resolved alongside the serum samples for comparison.