Encapsulation of phosphotriesterase within murine erythrocytes. Academic Article

abstract

• A new conceptual approach was employed to antagonize organophosphorus intoxication by using resealed carrier erythrocytes containing a recombinant phosphotriesterase. This enzyme has been reported to hydrolyze many organophosphorus compounds, including paraoxon, a potent cholinesterase inhibitor. Paraoxon is rapidly hydrolyzed by this enzyme to p-nitrophenol and diethylphosphate. Incorporation of phosphotriesterase within resealed murine erythrocytes was accomplished by hypotonic dialysis. The properties of this enzyme within these resealed erythrocytes were investigated. Addition of paraoxon to reaction mixtures containing these resealed erythrocytes loaded with phosphotriesterase resulted in the rapid hydrolysis of paraoxon. Hydrolysis of paraoxon did not occur when these carrier erythrocytes contained no phosphotriesterase. These in vitro studies suggest that carrier erythrocytes may be developed as an approach for the prophylactic and therapeutic antagonism of organophosphorus intoxication.

authors

• Raushel, Frank

published proceedings

• Toxicol Appl Pharmacol

altmetric score

• 3

author list (cited authors)

• Pei, L., Omburo, G., McGuinn, W. D., Petrikovics, I., Dave, K., Raushel, F. M., ... Way, J. L.

citation count

• 37

complete list of authors

• Pei, L||Omburo, G||McGuinn, WD||Petrikovics, I||Dave, K||Raushel, FM||Wild, JR||DeLoach, JR||Way, JL

publication date

• February 1994

publisher

• Elsevier  Publisher

published in

• TOXICOLOGY AND APPLIED PHARMACOLOGY  Journal

keywords

• Animals
• Aryldialkylphosphatase
• Drug Carriers
• Erythrocytes
• Esterases
• Hydrolysis
• Mice
• Paraoxon

Digital Object Identifier (DOI)

• 10.1006/taap.1994.1035

start page

• 296

end page

• 301

volume

• 124

issue

• 2

URL

• http://dx.doi.org/10.1006/taap.1994.1035