Geyer_2008_Chem.Biol.Interact_175_376

Reference

Title : Increased organophosphate scavenging in a butyrylcholinesterase mutant - Geyer_2008_Chem.Biol.Interact_175_376
Author(s) : Geyer BC , Woods RR , Mor TS
Ref : Chemico-Biological Interactions , 175 :376 , 2008
Abstract :

Nicotiana benthamiana plant lines expressing a reengineered human butyrylcholinesterase (BChE) with enhanced cocaine hydrolase activity were created. Subsequent purification and biochemical analysis revealed that compared to wild-type butyrylcholinesterase, the cocaine hydrolase displayed increased affinity to the organophosphate (OP) pesticides paraoxon (6.8 4x 10(-10)M vs. 1.11 x 10(-8)M) and malaoxon (9.81 x 10(-8)M vs. 5.99 x 10(-7)M). Furthermore, the cocaine hydrolase retained identical anticholinesterase binding profiles for all other compounds tested. Thus we have demonstrated a potential large-scale production platform for a multivalent antidote for cocaine and anticholinesterase poisoning.

PubMedSearch : Geyer_2008_Chem.Biol.Interact_175_376
PubMedID: 18514178

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Citations formats

Geyer BC, Woods RR, Mor TS (2008)
Increased organophosphate scavenging in a butyrylcholinesterase mutant
Chemico-Biological Interactions 175 :376

Geyer BC, Woods RR, Mor TS (2008)
Chemico-Biological Interactions 175 :376