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

dc.contributor.author	Comakli, Veysel
dc.contributor.author	Yerlikaya, Emrah
dc.contributor.author	Demirdag, Ramazan
dc.contributor.author	Kufrevioglu, Omer Irfan
dc.date.accessioned	2019-11-18T12:07:24Z
dc.date.available	2019-11-18T12:07:24Z
dc.date.issued	2012
dc.department	Belirlenecek
dc.description.abstract	Sheep 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 ºC, 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.
dc.identifier.uri	https://hdl.handle.net/20.500.12604/1623
dc.language.iso	en
dc.relation.publicationcategory	Uluslararası Editör Denetimli Dergi Makalesi
dc.rights	info:eu-repo/semantics/openAccess
dc.snmz	#KayıtKontrol#
dc.subject	Characterization, Carbonic anhydrase (CA), Sheep, Liver, Inhibition.
dc.title	Purification and Characterization of a-Carbonic Anhydrase II from Sheep Liver and Examining the Inhibition Effect of Kanamycin on Enzyme Activity
dc.type	Article

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