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dc.contributor.authorKoçyiğit, Ü.M. and Durna Daştan, S. and Taslimi, P. and Daştan, T. and Gülçin, İ.
dc.date.accessioned2021-04-08T12:07:41Z
dc.date.available2021-04-08T12:07:41Z
dc.date.issued2018
dc.identifier10.1002/jbt.22000
dc.identifier.issn10956670
dc.identifier.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-85040702304&doi=10.1002%2fjbt.22000&partnerID=40&md5=1f3097bc68097d1d014544c26091aed7
dc.identifier.urihttp://acikerisim.bingol.edu.tr/handle/20.500.12898/4412
dc.description.abstractIn 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. © 2017 Wiley Periodicals, Inc.
dc.language.isoEnglish
dc.sourceJournal of Biochemical and Molecular Toxicology
dc.titleInhibitory effects of some drugs on carbonic anhydrase enzyme purified from Kangal Akkaraman sheep in Sivas, Turkey


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