Purification of PON1 from human serum and assessment of enzyme kinetics against metal toxicity


Ekinci D., Beydemir Ş.

Biological Trace Element Research, cilt.135, sa.1-3, ss.112-120, 2010 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 135 Sayı: 1-3
  • Basım Tarihi: 2010
  • Doi Numarası: 10.1007/s12011-009-8500-0
  • Dergi Adı: Biological Trace Element Research
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.112-120
  • Anahtar Kelimeler: Inhibition, Metal toxicology, Paraoxonase
  • Ondokuz Mayıs Üniversitesi Adresli: Evet

Özet

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. © 2009 Humana Press Inc.