Akademik Veri Yönetim Sistemi
REVUE DE MEDECINE VETERINAIRE, cilt.158, ss.431-436, 2007 (SCI-Expanded, Scopus)
The buffalo erythrocyte glucose-6-phosphate dehydrogenase (EC 1.1.1.49, G6PD) was purified using 2', 5'-ADP Sepharose 4B affinity chromatography. During the overall purification steps, enzyme fractions having a specific activity of 63.33 U/mg proteins were concentrated 781.8-fold with a yield of 43.84%, and the enzyme purity was confirmed by SDS-PAGE (a single band of similar to 65 kDa). Then, some important drugs (Streptomycin, Vancomycin hydrochloride, Nafcillin and Dexamethasone) were investigated for in vitro enzyme inhibition, throughout determination of drugs IC50 values plotting % of activity vs. drug concentrations. According to IC50 values, dexamethasone and streptomycin were the most potent inhibitors (2.68 mM and 6.58 mM respectively) whereas Vancomycin hydrochloride exhibited moderate effects (IC50: 8.10 mM) and the Nafcillin inhibition was minimal (IC50: 18.24 mM). Besides, streptomycin and dexamethasone acted as allosteric inhibitors according to Lineweaver-Burk graphs with low Ki constants (2.225 +/- 0.409 mM and 1.649 +/- 0.269 mM respectively). The involvement of the G6PD inhibition during the drug toxicity discussed was then discussed.