Akademik Veri Yönetim Sistemi
ASIAN JOURNAL OF CHEMISTRY, cilt.21, sa.7, ss.5117-5122, 2009 (SCI-Expanded)
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 V(max) values for the same substrate were obtained by means of Linewearver-Burk graphics. The purification degree for bovine bone marrow was calculated. The V(max) and K(M) values at optimum pH and at 20 degrees C for the substrate (p-nitrophenyl acetate) were 120.418 mu mol/L min and 2.409 x 10(-3) mM, respectively. The K(1) and I(50) values for sulfanilamide, KSCN, NaN(3) and acetazolamide were determined in bovine bone marrow carbonic anhydrase.