Siirt Tiftik Keçisi Böbrek Dokusundan Karbonik Anhidraz Enziminin Saflaştırılması, Karakterizasyonu ve Bazı Biyokimyasal Özelliklerinin Araştırılması
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Tarih
2016
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Dergi ISSN
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Yayıncı
Erişim Hakkı
info:eu-repo/semantics/openAccess
Özet
Carbonic anhydrase (CA) (E.C:4.2.1.1) is a group of metalloenzyme containing zinc widely distributed from the simplest organisms such as bacteria to the most complex organisms such as plants and animals. CA inhibitors are some of the principal drugs used in the management of canine and feline glaucoma. In earlier studies; CA enzymes successfully have been purified and characterized from many living things such as; sheep, chicken, fish, bovine and human. In this study, the CA enzyme has purified from Siirt Mohair Goat kidney tissue with 902.9 EU x mg-1 of specific activity, 50.19% of purification yield and 83.54 of purification folds by using Sepharose-4B-L-tyrosine-sulfonamide affinity column. The purity of the purified enzyme has confirmed by SDS-PAGE. As the characterization of CA enzyme’s in Siirt Mohair Goat kidney has been done; the optimum ionic strength=25mM, the optimum pH=8.5, the optimum temperature=45ºC and the stable pH=7.0 has been determined. Inhibitory effects of Al3+, Ni2+, Cd2+, Pb2+, Ba2+, Zn2+, B3+, Fe3+, Se2+, Ag+ and Co2+ metal ions have been examined on the purified CA enzyme. Inhibition graphics have been drawn in order to find the IC50 values of metals showing inhibition.
Açıklama
Anahtar Kelimeler
Affinity, Metal Ion, Enzyme, Inhibition, Kidney.
