Partial Purification and Some Interesting Properties of Glutathione Peroxidase from Liver of Camel (Camelus dromedarius)

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dc.authorid57190409749
dc.authorid6507478596
dc.authorid56400331100
dc.authorid57201282307
dc.authorid7004132795
dc.contributor.authorChafik A.
dc.contributor.authorEssamadi A.
dc.contributor.authorÇelik S.Y.
dc.contributor.authorSolak K.
dc.contributor.authorMavi A.
dc.date.accessioned20.04.201910:49:12
dc.date.accessioned2019-04-20T21:43:11Z
dc.date.available20.04.201910:49:12
dc.date.available2019-04-20T21:43:11Z
dc.date.issued2018
dc.departmentBayburt Üniversitesien_US
dc.description.abstractClimate change and increasing temperatures are global concerns. Well adapted to desert life, the camel (Camelus dromedarius) lives most of its life under high environmental stress and represents an ideal model for studying desert adaptation among mammals. Glutathione peroxidase is the principal antioxidant defense system capable of protecting cells from oxidative stress. Glutathione Peroxidase from camel liver was purified (11.64-fold purification with 1.73% yield) and characterized The molecular weight of the enzyme was estimated to be about 69 kDa by gel filtration and 34 kDa by SDS-PAGE, implying dimeric structure of the protein. An optimum temperature of 47°C and an optimum pH of 7.8 were found. This enzyme is a typical SH-enzyme that is inhibited by D,L-dithiothreitol and ?-mercaptoethanol and sensitive to bivalent cations. The enzyme had common specificity toward hydroperoxides and high specificity for reduced glutathione. The Km and Vmax values for hydrogen peroxide and reduced glutathione were 0.57 and 2.10 mM and 1.11 and 0.87 U/mg, respectively. The purified enzyme contained 16 ng of selenium per mg of protein. Our results show that the camel glutathione peroxidse exhibits properties different of those reported for other mammalian species. Lower molecular weight, homodimeric structure, higher optimum temperature, relatively low optimum pH, high affinity for hydrogen peroxide at low concentration of reduced glutathione and very low content of selenium could be explained by adaptation of the camel to living in the desert under intense environmental stress. © 2018, Pleiades Publishing, Ltd.en_US
dc.identifier.doi10.1134/S1068162018010041
dc.identifier.endpage51
dc.identifier.issn1068-1620
dc.identifier.issue1
dc.identifier.scopus2-s2.0-85043993604en_US
dc.identifier.scopusqualityQ4en_US
dc.identifier.startpage41
dc.identifier.urihttps://dx.doi.org/10.1134/S1068162018010041
dc.identifier.urihttps://hdl.handle.net/20.500.12403/444
dc.identifier.volume44
dc.identifier.wosWOS:000427499200004en_US
dc.identifier.wosqualityQ4en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.language.isoenen_US
dc.publisherPleiades Publishing
dc.relation.ispartofRussian Journal of Bioorganic Chemistryen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectadaptation
dc.subjectcamel
dc.subjectdesert
dc.subjectglutathione peroxidase
dc.subjectliver
dc.subjectadaptation
dc.subjectcamel
dc.subjectdesert
dc.subjectglutathione peroxidase
dc.subjectliver
dc.titlePartial Purification and Some Interesting Properties of Glutathione Peroxidase from Liver of Camel (Camelus dromedarius)en_US
dc.typeArticleen_US

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