An alternative purification method for human serum paraoxonase 1 and its interactions with anabolic compounds

Demir D., Gencer N., Arslan O.

JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, vol.31, no.2, pp.247-252, 2016 (Peer-Reviewed Journal) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 31 Issue: 2
  • Publication Date: 2016
  • Doi Number: 10.3109/14756366.2015.1018242
  • Journal Indexes: Science Citation Index Expanded, Scopus
  • Page Numbers: pp.247-252


In this study, an alternative purification method for human paraoxonase 1 (hPON1) enzyme was developed using two-step procedures, namely, ammonium sulfate precipitation and Sepharose-4B-l-tyrosine-3-aminophenantrene hydrophobic interaction chromatography. SDS-polyacrylamide gel electrophoresis of the enzyme indicates a single band with an apparent M-W of 43kDa. The enzyme was purified 219-fold with a final specific activity of 4408400 U/mg and a yield of 10%. Furthermore, we examined the in vitro effects of some anabolic compounds, such as zeranol, 17 beta-estradiol, diethylstilbestrol, oxytocin, and trenbolone on the enzyme activity to understand the better inhibitory properties of these molecules. The five anabolic compounds dose dependently decreased the activity of hPON1 with inhibition constants in the millimolar-micromolar range. The results show that these compounds exhibit inhibitory effects on hPON1 at low concentrations with IC50 values ranging from 0.064 to 16.900 mu M.