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Purification of PON1 from Human Serum and Assessment of Enzyme Kinetics Against Metal Toxicity

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Abstract

Paraoxonase-1 (PON1) is an organophosphate hydrolyser enzyme which has also antioxidant properties in metabolism. Due to its crucial functions, inhibition of the enzyme is undesirable and very dangerous. PON1 enzyme activity should not be altered in any case. Inhibitory investigations of this enzyme are therefore important and useful. Metal toxicology of enzymes has become popular in the recent years. Here, we report the in vitro inhibitory effects of some metal ions, including Pb+2, Cr+2, Fe+2, and Zn+2, on the activity of human serum PON1 (hPON1; EC 3.1.8.1.). For this purpose, we purified the enzyme from human serum and analyzed the alterations in the enzyme activity in the presence of metal ions. The results show that metal ions exhibit inhibitory effects on hPON1 at low concentrations with IC 50 values ranging from 0.838 to 7.410 mM. Metal ions showed different inhibition mechanisms: lead and iron were competitive, chrome was noncompetitive, and zinc was uncompetitive. Lead was determined to be the most effective inhibitor.

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Abbreviations

PON1:

Paraoxonase-1

OPs:

Organophosphates

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Authors and Affiliations

  1. Department of Chemistry, Science Faculty, Biochemistry Division, Atatürk University, 25240, Erzurum, Turkey

    Deniz Ekinci & Şükrü Beydemir

  2. Biotechnology Application and Research Center, Atatürk University, 25240, Erzurum, Turkey

    Şükrü Beydemir

Authors
  1. Deniz Ekinci
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  2. Şükrü Beydemir
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Correspondence to Şükrü Beydemir.

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Ekinci, D., Beydemir, Ş. Purification of PON1 from Human Serum and Assessment of Enzyme Kinetics Against Metal Toxicity. Biol Trace Elem Res 135, 112–120 (2010). https://doi.org/10.1007/s12011-009-8500-0

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  • DOI: https://doi.org/10.1007/s12011-009-8500-0

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