Koyun Karaciğerinden a-Karbonik Anhidraz II’ nin Saflaştırılması ve Karakterizasyonu ve Enzim Aktivitesi Üzerine Kanamisinin İnhibisyon Etkisinin İncelenmesi

Year 2012, Volume: 40 Issue: 2, 133 - 138, 01.04.2012

Veysel Çomaklı Emrah Yerlikaya Ramazan Demirdağ Ömer İrfan Küfrevioğlu

Abstract

K oyun karbonik anhidraz-II E.C: 4.2.1.1 enzimi koyun karaciğerinden saflaştırıldı ve bazı karakteristik özellikleri araştırıldı. Enzim 4000 EU/mg protein spesifik aktivitesi ve % 38.6 verim ile yaklaşık olarak 43,1 kat saflaştırıldı. Enzim için optimum pH, optimum sıcaklık, optimum iyonik şiddet ve stabil pH sırasıyla 7.5, 40ºC, 10 mM ve 8.5 olarak belirlendi. Moleküler ağırlığı sodyum dodesil sülfat poliakrilamid jel elektroforezi ile 29 kDa olarak bulundu. Kanamisinin enzim aktivitesi üzerine in vitro inhibitör etkisi incelendi

Keywords

Karakterizasyon, Karbonik Anhidraz, Koyun, Karaciğer, İnhibisyon.

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

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, 40ºC, 10 mM and 8.5, respectively. The molecular weight was found 29 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis SDS-PAGE . Kanamycin ex- hibited in vitro inhibitory effect on the enzyme activity.

Keywords

characterization, Carbonic anhydrase CA, Sheep, Liver, Inhibition.

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