CARBONIC ANYHDRASE ENZYME FROM THE SIIRT MOHAIR GOAT LIVER : PURIFICATION, CHARACTERIZATION AND ASSESSMENT OF ENZYME KINETICS AGAINST METAL TOXICITY

ABSTRACT Because 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 many living things 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= 40 oC and the stable pH= 7.0 has been determined. Inhibitory effects of some metal ions have been examined on the purified CA enzyme.   Keywords: Affinity, Metal Ions, Inhibition, Siirt Mohair Goat.     OZET Fizyolojik ve klinik rollerinden dolayi karbonik anhidrazlar (CAs), en cok incelenen enzimlerdir. Daha onceki calismalarda CA enzimleri kopek, domuz, koyun, tavuk, ari, balik, sigir, bakteri ve insan gibi bircok canlidan saflastirilmis ve karakterize edilmistir. Bu calismada da CA enzimi Siirt Tiftik Kecisi karaciger dokusundan 1930,84 EU x mg-1 spesifik aktivite ile % 57,28 verimle 80,55 kat saflastirildi. Saflastirilan enzimin safligi SDS-PAGE ile dogrulandi. Siirt Tiftik Kecisi karacigerinden CA enziminin karakterizasyonu yapildiginda; optimum iyonik siddet=25 mM, optimum pH= 8.0, optimum sicaklik= 40 oC ve stabil pH = 7.0 olarak belirlendi. Saflastirilmis CA enzimi uzerine bazi metal iyonlarinin inhibitor etkileri incelendi.   Anahtar Kelimeler: Afinite, Metal Iyonlari, Inhibisyon, Siirt Tiftik Kecisi.