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Article

The ratio of serum paraoxonase/arylesterase activity using an improved assay for arylesterase activity to discriminate PON1(R192) from PON1(Q192).

Journal of atherosclerosis and thrombosis - 1 Jan 2003

Nakanishi Mamoru, Takanami Yoshikazu, Maruyama Taro, Murata Mitsuru, Motohashi Yoshiko, Nakano Satomi, Uchida Kagehiro, Maruyama Chizuko, Kyotani Shingo, Tsushima Motoo

Abstract excerpt

Human serum paraoxonase (PON1) exists in 2 major polymorphic forms: Q (glutamine) or R (arginine) at codon 192. The PON1(192) activity polymorphism is substrate dependent. The PON1(Q192) isoform has a higher rate of in vitro hydrolysis of diazoxon, sarin, and soman, whereas the PON1(R192) isoform has higher activity for the hydrolysis of paraoxon and chlorpyrifos oxon. Both isoforms hydrolyze phenyl acetate at...

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Identifiers

PMID: 15037822
DOI: 10.5551/jat.10.337

Genes

PON1

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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The ratio of serum paraoxonase/arylesterase activity using an improved assay for arylesterase activity to discriminate PON1(R192) from PON1(Q192).PMID 15037822Read ↗

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