Purification and characterization of carbonic anhydrase enzyme from sheep heart tissue andinvestigation of the effects of new synthesized sulfonamide chalcones

In this study, sheep heart tissue was purified using Sepharose-4B-L-tyrosine-sulfanilamide affinity chromatography with a specific activity of 900 EU / mg and a yield of 46.15% and a purification coefficient of 51.93. SDS-polyacrylamide gel electrophoresis was performed to check the purity of the purified enzyme and a single band was observed. The molecular mass for the isoenzymia of the sheep heart was determined to be 31 kDa. In addition, optimum ionic strength, optimum pH and stabilization pH values were determined in the characterization studies performed for this enzyme. In this thesis, new sulfonamide chalcone containing azo group is synthesized. The characterization of the synthesized new compounds was determined by means of spectroscopic methods such as NMR, MS, FT-IR and elemental analysis. IC50 values for novel azo sulphonamide chalcone synthesized by the inhibitory effect on sheep heart enzyme were determined.