Purification and Characterization of a-Carbonic Anhydrase II from Sheep Liver and Examining the Inhibition Effect of Kanamycin on Enzyme Activity

dc.contributor.authorComakli, Veysel
dc.contributor.authorYerlikaya, Emrah
dc.contributor.authorDemirdag, Ramazan
dc.contributor.authorKufrevioglu, Omer Irfan
dc.date.accessioned2019-11-18T12:07:24Z
dc.date.available2019-11-18T12:07:24Z
dc.date.issued2012
dc.departmentBelirleneceken_US
dc.description.abstractSheep carbonic anhydrase - II (SCA-II) (E.C: 4.2.1.1) was purified from sheep liver and some characteristic properties were investigated. The enzyme was purified approximate 43.1-fold with a yield of 38.6%, and a specific activity of 4000 EU/mg proteins. For the enzyme, optimum pH, optimum temperature, optimum ionic strength and stable pH were determined to be 7.5, 40 ÂșC, 10 mM and 8.5, respectively. The molecular weight was found 29 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Kanamycin exhibited in vitro inhibitory effect on the enzyme activity.en_US
dc.identifier.urihttps://hdl.handle.net/20.500.12604/1623
dc.language.isoenen_US
dc.relation.publicationcategoryUluslararası Editör Denetimli Dergi Makalesien_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.snmz#KayıtKontrol#
dc.subjectCharacterization, Carbonic anhydrase (CA), Sheep, Liver, Inhibition.en_US
dc.titlePurification and Characterization of a-Carbonic Anhydrase II from Sheep Liver and Examining the Inhibition Effect of Kanamycin on Enzyme Activityen_US
dc.typeArticleen_US

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