Human and rabbit paraoxonases: Purification, cloning, sequencing, mapping and role of polymorphism in organophosphate detoxification
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Cited by (117)
Effect of calcium channel blockers on paraoxonase-1 (PON1) activity and oxidative stress
2014, Pharmacological ReportsCitation Excerpt :This purification procedure, which is relatively fast, was developed by our group [6,27–29,45]. The results of the purification studies were similar to those in our previous reports and other studies [5,6,27–29,33,34,45,62,69]. SDS-polyacrylamide gel electrophoresis (SDS-PAGE) was performed to confirm the purity of the enzyme.
Paraoxonase-1, an organophosphate detoxifier and cardioprotective enzyme, is inhibited by anesthetics: An in vitro and in vivo insight
2011, Pesticide Biochemistry and PhysiologyIn vitro efficacy of paraoxonase 1 from multiple sources against various organophosphates
2011, Toxicology in VitroProtective efficacy of catalytic bioscavenger, paraoxonase 1 against sarin and soman exposure in guinea pigs
2011, Biochemical PharmacologyCitation Excerpt :The secreted human blood PON1 enzyme is 355 amino acids long with a molecular mass in the range of 43–45 kDa [16,17]. On the other hand, rabbit serum PON1 is a 359 amino acid long protein with 85% identity to human serum PON1 [18–20]. Both human and rabbit serum PON1 exhibit multiple types of polymorphisms which affect the catalytic activity of the enzyme [21–23].
Pharmacological and dietary modulators of paraoxonase 1 (PON1) activity and expression: The hunt goes on
2011, Biochemical PharmacologyDifferential hydrolysis of homocysteine thiolactone by purified human serum <sup>192</sup>Q and <sup>192</sup>R PON1 isoenzymes
2011, Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences
Copyright © 1993 Published by Elsevier Ireland Ltd.