Some cardiovascular therapeutics inhibit paraoxonase 1 (PON1) from human serum

İşgör, Mehmet Mustafa; Beydemır, Şükrü

doi:10.1016/j.ejphar.2010.07.030

Cited by 45 publications

(22 citation statements)

References 55 publications

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“…PON1 with 354 amino acids has three activities including paraoxonase, arylesterase and diazoxon activities 14 . The enzyme is called as paraoxonase since it was first characterized as a hydrolyzer for OPs including paraoxon and its physiological substrate is unknown.…”

Section: Research Articlementioning

confidence: 99%

Synthesis and paroxonase activities of novel bromophenols

Akbaba

Türkeş

Polat

et al. 2012

Journal of Enzyme Inhibition and Medicinal Chemistry

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Section: Research Articlementioning

confidence: 99%

Synthesis and paroxonase activities of novel bromophenols

Akbaba

Türkeş

Polat

et al. 2012

Journal of Enzyme Inhibition and Medicinal Chemistry

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“…PON1 has three activities: paraoxonase, arylesterase, and diazoxon. 7 The enzyme can hydrolyze O-P ester linkage in paraoxon by its esterase activitiy. 29,30 It is known that paraoxon is used as an insecticide, due to its strong inhibitory action against acetylcholine esterase.…”

Section: Discussionmentioning

confidence: 99%

“…However, it can also catalyze the cleavage of ester bonds. 7 As a matter of fact, PON1 had been initially characterized as a hydrolyzer for organophosphates including paraoxon. The enzyme got its name from this reaction.…”

Section: 3mentioning

confidence: 99%

Purification, refolding, and characterization of recombinant human paraoxonase-1

Demir¹,

Beydemır²

2015

Turk J Chem

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Abstract:A high density lipoprotein (HDL)-linked enzyme with antioxidant and antiatherogenic properties, paraoxonase-1(PON1), prevents the formation of atherosclerotic lesions in humans. In the present study, a recombinant hPON1 gene was produced using a small ubiquitin-related modifier (SUMO) fusion protein expression system. To that end, the hPON1 gene was amplified from human liver-ready cDNA, cloned into the expression vector pET SUMO, and expressed in Escherichia coli BL21 (DE3). The predominance of the expressed fusion SUMO-hPON1 protein was inclusion bodies and purified using 6xHis affinity chromatography under natural and denaturing conditions. Subsequently, the enzyme was purified and refolded directly on the affinity matrix under redox conditions to obtain a bioactive protein in a single step. The inclusion bodies were solubilized with urea, guanidine hydrochloride, and Triton X-100 and refolded in vitro. After purification, 0.045 mg/mL protein in soluble fraction and 0.108 mg/mL protein from inclusion bodies were obtained. Optimum temperature, pH, and ionic strength for rhPON1 activity were determined as 40• C, 10.0, and 100 mM, respectively. The kinetic parameters K m and V max for rhPON1 were determined as 0.94 mM and 110.01 EU/mL, respectively, by using Lineweaver-Burk plots.

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“…For instance, inhibition and activation effects of various drugs on the activities of different enzymes have been studied in our laboratory up to now. [30][31][32][33][34][35][36][37][38][39] Considering the above mentioned information, we aimed in the present study to purify PON1 from human serum and to investigate the kinetic interactions between the enzyme and some antibiotic drugs, namely oxytetracycline hydrochloride, netilmycin sulfate, lincomycin hydrochloride, clindamycin phosphate, streptomycin sulfate. To this end, hPON1 was purified using simple methods.…”

Section: Discussionmentioning

confidence: 99%