Inhibitory effects of some drugs on carbonic anhydrase enzyme purified from Kangal Akkaraman sheep in Sivas,Turkey |
| |
Authors: | Ümit M. Koçyiğit Sevgi Durna Daştan Parham Taslimi Taner Daştan İlhami Gülçin |
| |
Affiliation: | 1. Vocational School of Health Services, Cumhuriyet University, Sivas 58140, Turkey;2. Department of Animal Nutrition and Zootechnics, Division of Biometry and Genetics, Faculty of Veterinary Medicine, Cumhuriyet University, Sivas 58140, Turkey;3. Department of Chemistry, Faculty of Sciences, Atatürk University, Erzurum 25240, Turkey;4. Department of Chemistry, Faculty of Arts and Sciences, Bingol University, Bingol 12000, Turkey |
| |
Abstract: | In this study, carbonic anhydrase (CA) enzyme was purified and characterized from blood samples of Kangal Akkaraman sheep and inhibitory properties on certain antibiotics were examined. CA purification was composed of preparation of the hemolysate and conducting the Sepharose‐4B‐tyrosine‐sulfanilamide affinity gel chromatography in having specific activity of 11626 EU mg?1, yield of 14.40%, and 242.76‐fold purification. Sodium dodecyl sulfate‐polyacrylamide gel electrophoresis was performed to assess the enzyme purity and a single band was observed. Some antibiotics were exhibited in vitro inhibition on the CA activity. IC50 values of these inhibitors were calculated by plotting activity percentage. IC50 values of certain drugs (dexamethasone; caffeine; metamizole sodium; tetramisol; ceftiofur HCl; ivermectin; tavilin 50; penokain G; neosym; and sulfamezathine) were found as 0.38, 8.24, 285.53, 114.77, 5.33, 2.76, 27.58, 213.50, 208.28, and 36.60 μM, respectively. Ki values of different drugs on Kangal Akkaraman sheep blood CA activity were found in the range of 0.21 ± 0.038–266.64 ± 37.11 μM. |
| |
Keywords: | carbonic anhydrase drugs enzyme purification enzyme inhibition Kangal Akkaraman sheep |
|
|