In this work, the carbonic anhydrase was purified from bovine bone marrow and investigated its kinetic properties. Carbonic anhydrase was purified from bovine bone marrow using affinity chromatography by sepharose 4B-L-tyrosine sulphanilamide. During purification steps, the activity of enzyme was measured using p-nitrophenyl acetate at pH: 7.4. Optimum pH and optimum temperature values for bovine bone marrow carbonic anhydrase were determined and then K m and Vmax values for the same substrate were obtained by means of Linewearver-Burk graphics. The purification degree for bovine bone marrow was calculated. The Vmax, and Km values at optimum pH and at 20 °C for the substrate (p-nitrophenyl acetate) were 120.418 u?mol/L min and 2.409 x 103 mM, respectively. The K1 and I50 values for sulfanilamide, KSCN, NaN3 and acetazolamide were determined in bovine bone marrow carbonic anhydrase
