ArticleThe Biochemical journal2003
Identification of paraoxonase 3 in rat liver microsomes: purification and biochemical properties.
Article in The Biochemical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 41 citations in OpenAlex.
- Unlocking Lactonase Enzymes as Biocatalysts for the Deracemisation of Chiral γ-Thiolactones.Angewandte Chemie (International ed. in English) · 2025Article
- Astragalus Injection Modulates the Pharmacokinetics of Doxorubicin and CYP450 Enzymes.Current pharmaceutical design · 2025Article
- A PON for All Seasons: Comparing Paraoxonase Enzyme Substrates, Activity and Action including the Role of PON3 in Health and Disease.Antioxidants (Basel, Switzerland) · 2022Review
- The Structure and Function of Paraoxonase-1 and Its Comparison to Paraoxonase-2 and -3.Molecules (Basel, Switzerland) · 2020Review
- Paraoxonase 3: Structure and Its Role in Pathophysiology of Coronary Artery Disease.Biomolecules · 2019Review
- Impact of antibacterial drugs on human serum paraoxonase-1 (hPON1) activity: an in vitro study.Asian Pacific journal of tropical biomedicine · 2014Article
- The human paraoxonase gene cluster as a target in the treatment of atherosclerosis.Antioxidants & redox signaling · 2012Review
- Modulation of paraoxonase 1 and 3 expression after moderate exercise training in the rat.Journal of lipid research · 2009Article
- Effect of pre-germinated brown rice intake on diabetic neuropathy in streptozotocin-induced diabetic rats.Nutrition & metabolism · 2007Article
- Pharmacogenetics of paraoxonases: a brief review.Naunyn-Schmiedeberg's archives of pharmacology · 2004Review
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Three paraoxonase genes (PON1, PON2 and PON3) have been described so far in mammals. Although considerable information is available regarding PON1, little is known about PON2 and PON3. PON3 has been isolated recently from rabbit serum [Draganov, Stetson, Watson, Billecke and La Du (2000) J. Biol. Chem. 275, 33435-33442] and liver [Ozols (1999) Biochem. J. 338, 265-275]. In the present study, we have identified the presence of PON3 in rat liver microsomes and a method for the purification to homogeneity is presented. PON3 has been purified 177-fold to apparent homogeneity with a final specific activity of 461 units/mg using a method consisting of seven steps: solubilization of the microsomal fraction, hydroxyapatite adsorption, chromatography on DEAE-Sepharose CL-6B, non-specific affinity chromatography on Cibacron Blue 3GA, two DEAE-cellulose steps and a final affinity chromatography on concanavalin A-Sepharose. SDS/PAGE of the final preparation indicated a single protein-staining band with an apparent molecular mass of 43 kDa. The isolated protein was identified by nanoelectrospray MS. Internal amino acid sequences of several peptides were determined and compared with those of human, rabbit and mouse PON3, showing a high similarity. Some biochemical properties of PON3 were also studied, including optimum pH, K(m) and heat and pH stability.
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