Carbonic Anyhdrase Enzyme From The Siirt Mohair Goat Liver :Purification, Characterization and Assessment of Enzyme Kinetics Against Metal Toxicity

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dc.contributor.authorYerlikaya, Emrah
dc.contributor.authorKaragecili, Hasan
dc.contributor.authorDemirdag, Ramazan
dc.contributor.authorKaya, Mustafa Oguzhan
dc.date.accessioned2019-11-18T12:15:47Z
dc.date.available2019-11-18T12:15:47Z
dc.date.issued2017
dc.departmentBelirleneceken_US
dc.description.abstractBecause of their physiological and clinical roles, carbonic anhydrases (CAs) are the most studied enzymes. In earlier studies; CA enzymes have been purified and characterized from the tissues and erythrocytes of many organisms such as; dog, swine, sheep, chicken, bee, fish, bovine, bacteria and human. In this study, the CA enzyme has purified from Siirt Mohair Goat liver tissue with 1930.84 EU x mg-1 of specific activity, 57.28% of purification yield and 80.55 of purification folds. The purity of the purified enzyme has confirmed by SDS-PAGE. As the characterization of CA enzyme’s in Siirt Mohair Goat liver has been done; the optimum ionic strength=25 mM, the optimum pH= 8.0, the optimum temperature= 40ºC and the stable pH= 7.0 has been determined. Inhibitory effects of some metal ions have been examined on the purified CA enzyme. IC50 values of inhibiting metal ions were found as 2.24, 2.76, 2.36, 3.20, 2.55, 2.25, 3.28, 2.13, 3.10, 1.75, 2.16 and 3.50 mM for Al3+, Ni2+, Cd2+, Cu2+, Pb2+, Ba2+, Zn2+, B3+, Fe3+, Se2+, Ag+ and Co2+ respectively. As a result, CA enzyme was first purified from theen_US
dc.identifier.urihttps://hdl.handle.net/20.500.12604/1626
dc.language.isoenen_US
dc.relation.publicationcategoryUlusal Hakemli Dergi Makalesien_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.snmz#KayıtKontrol#
dc.subjectAffinity, Metal Ions, Inhibition, Siirt Mohair Goat.en_US
dc.titleCarbonic Anyhdrase Enzyme From The Siirt Mohair Goat Liver :Purification, Characterization and Assessment of Enzyme Kinetics Against Metal Toxicityen_US
dc.typeArticleen_US

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