Purification and characterization of paraoxonase 1 (PON1) from swiss black, holstein, and montofon bovines

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dc.contributor.authorErzengin, Mahmut
dc.contributor.authorDemir, Dudu
dc.contributor.authorArslan, Mikail
dc.contributor.authorSinan, Selma
dc.date.accessioned13.07.201910:50:10
dc.date.accessioned2019-07-16T09:15:47Z
dc.date.available13.07.201910:50:10
dc.date.available2019-07-16T09:15:47Z
dc.date.issued2014
dc.departmentSabire Yazıcı Fen Edebiyat Fakültesi
dc.description.abstractParaoxonase 1 (PON1: EC 3.1.8.1) is a calcium-dependent enzyme associated with high-density lipoproteins (HDLs) and has a protective effect against oxidation of low-density lipoproteins (LDLs) in mammals. PON1 is the best-studied member of a family of enzymes called serum paraoxonases, or PONs, identified in mammals and other vertebrates as well as in invertebrates. PONs exhibit a range of important activities, including drug metabolism and detoxification of organophosphates such as nerve agents. This study reports, for the first time, purification and biochemical characterization of serum PON1 from different bovine breeds namely Swiss Black, Holstein, and Montofon. Bovine serum PON1s were purified using ammonium sulfate precipitation followed by Sepharose-4B-l-tyrosine-1-naphthylamine hydrophobic interaction chromatography. SDS-polyacrylamide gel electrophoresis of the purified enzymes indicates a single band with an apparent MW of 43 kDa. The purified enzymes had a specific activity of 10.78, 27.00, and 22.38 U/mg for Swiss Black, Holstein, and Montofon bovines, respectively. The overall purification rates of our method were 262.47-, 2,476.90-, and 538.06-fold for Swiss Black, Holstein, and Montofon bovines, respectively. Furthermore, using phenyl acetate as a substrate, we determined the K (M) and V (max) values of the purified enzymes, as 0.80 mM, 1428.5 U/ml for Swiss Black; 0.40 mM, 714.3 U/ml for Holstein; and 0.50 mM, 1,111.1 U/ml for Montofon bovine. The present study has revealed that there is no substantial difference in PON1 activities among the studied bovine breeds.
dc.identifier.doi10.1007/s12010-014-0931-1
dc.identifier.endpage1606en_US
dc.identifier.issn0273-2289
dc.identifier.issn1559-0291
dc.identifier.issue7en_US
dc.identifier.pmid24907040
dc.identifier.scopusqualityQ2
dc.identifier.startpage1597en_US
dc.identifier.urihttps://doi.org/10.1007/s12010-014-0931-1
dc.identifier.urihttps://hdl.handle.net/20.500.12451/4465
dc.identifier.volume173en_US
dc.identifier.wosWOS:000340528300003
dc.identifier.wosqualityN/A
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.language.isoen
dc.publisherHumana Press
dc.relation.ispartofApplied Biochemistry and Biotechnology
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/embargoedAccess
dc.subjectBovine Serum
dc.subjectParaoxonase 1
dc.subjectHydrophobic Interaction Chromatography
dc.subjectSwiss Black
dc.subjectHolstein
dc.subjectMontofon
dc.titlePurification and characterization of paraoxonase 1 (PON1) from swiss black, holstein, and montofon bovines
dc.typeArticle

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