Purification, characterization, and investigation of in vitro inhibition by metals of paraoxonase from different sheep breeds

Abstract

Paraoxonase (PON) was purified and characterized from the Merino and Kivircik sheep's blood serums by a two-step procedure using ammonium sulphate precipitation and Sepharose-4B-L-tyrosine-1-napthylamine hydrophobic interaction chromatography for the first time. On SDS-polyacyrilamide gel electrophoresis, purified human serum paraoxonase yielded a single band of 66 kDa on SDS-PAGE. The K_M and V_max were 0.482 mM and 41.348 U/mL.dak for Merino PON enzyme, 0.153 mM and 70.289 U/mL.dak for Kivircik PON, respectively. The effect of Mn²⁺ , Hg²⁺ , Co²⁺ , Cd²⁺ , Ni²⁺ and Cu²⁺ heavy metals on purified Merino and Kivircik serum PON in vitro was determined.

Keywords::

• Paraoxonase
• heavy metals
• inhibition

Notice of Correction

The version of this article published online ahead of print on 04 Sept 2012 contained an error on page 6, The sentence “In addition to the studies above, there are investigations regarding the inhibitory effects Please close up space hereof metals on PON activity as well.” should have read “In addition to the studies above, there are investigations regarding the inhibitory effects of metals on PON activity as well.”. The error has been corrected for this version.