title: 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 KM and Vmax 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 Mn(2+) , Hg(2+) , Co(2+) , Cd(2+) , Ni(2+) and Cu(2+) heavy metals on purified Merino and Kivircik serum PON in vitro was determined.
authors.affiliation: Balikesir University, Science and Art Faculty Department of Chemistry, Balikesir, Turkey.
authors.forename: Kadir
authors.initials: K
authors.lastname: Erol
authors.forename: Nahit
authors.initials: N
authors.lastname: Gençer
authors.forename: Mikail
authors.initials: M
authors.lastname: Arslan
authors.forename: Oktay
authors.initials: O
authors.lastname: Arslan
mesh_terms: D000645:Ammonium Sulfate; D000818:Animals; D043303:Aryldialkylphosphatase / Q000037:antagonists & inhibitors / Q000097:blood / Q000302:isolation & purification*; D001798:Blood Proteins / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D002413:Cations, Divalent; D002847:Chromatography, Agarose; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007700:Kinetics; D034561:Sheep, Domestic; D013045:Species Specificity; D028561:Transition Elements / Q000737:chemistry*
chemical_list: D001798:Blood Proteins; D002413:Cations, Divalent; D028561:Transition Elements; D043303:Aryldialkylphosphatase; D000645:Ammonium Sulfate