期刊
JOURNAL OF BIOCHEMICAL AND MOLECULAR TOXICOLOGY
卷 32, 期 1, 页码 -出版社
WILEY
DOI: 10.1002/jbt.22000
关键词
carbonic anhydrase; drugs; enzyme purification; enzyme inhibition; Kangal Akkaraman sheep
资金
- Cumhuriyet University Research Fund (CUBAP) [SHMYO-011]
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 11626EUmg(-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 36.60M, respectively. K-i 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 mu M.
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