The subcellular localization and different biochemical properties of a human hepatic microsomal enzyme that hydrolyses paraoxon (paraoxonase, PON1) were studied and compared to the paraoxon hydrolase activity found in human plasma as well as in rat liver and plasma. Having evaluated the influence of
The active site of human paraoxonase (PON1)
β Scribed by Denis Josse; Oksana Lockridge; Weihua Xie; Cynthia F. Bartels; Lawrence M. Schopfer; Patrick Masson
- Publisher
- John Wiley and Sons
- Year
- 2001
- Tongue
- English
- Weight
- 83 KB
- Volume
- 21
- Category
- Article
- ISSN
- 0260-437X
- DOI
- 10.1002/jat.789
No coin nor oath required. For personal study only.
β¦ Synopsis
Ideally we would like to treat people exposed to nerve agents with an enzyme that rapidly destroys nerve agents. The enzymes considered for such a role include human butyrylcholinesterase (BChE), acetylcholinesterase (AChE), carboxylesterase and paraoxonase (PON1). Success has been achieved in endowing BChE with the ability to hydrolyze organophosphates. The G117H mutant of BCHE hydrolyzes sarin and VX, whereas the double mutant G117H/E197Q hydrolyzes soman (
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## Abstract Β© 2005 Wiley Periodicals, Inc. J Biochem Mol Toxicol 19:182β183, 2005; Published online in Wiley InterScience (www.interscience.wiley.com). DOI 10.1002/jbt.20079
## Abstract __Background__: Inhibition studies on PON1 as an organophosphateβhydrolyzing and atheroprotective enzyme could be useful in elucidating the function of PON1. This study is aimed at examining the in vitro effects of the flavonoid naringenin on PON1 activity in human serum and purified en
## Abstract Paraoxonase 1 (PON1), a highβdensity lipoproteinβassociated enzyme known to protect against cellular damage from toxic agents, may also have antioxidant properties. PON1 activity levels have been reported to differ by sex in human and animal studies with females exhibiting higher basal