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    Purification and Characterization of Carbonic Anhydrase from A. gri Balik Lake Trout Gill (Salmo trutta labrax) and Effects of Sulfonamides on Enzyme Activity
    (Wiley, 2015) Demirdag, Ramazan; Comakli, Veysal; Kuzu, Muslum; Yerlikaya, Emrah; Senturk, Murat
    Carbonic anhydrase (CA) was purified from Ar Balk Lake trout gill (fCA) by affinity chromatography on a sepharose 4B-tyrosine-sulfanilamide column. The fCA enzyme was purified with about a 303.9 purification factor, a specific activity 4130.4 EU (mg-protein)(-1), and a yield of 79.3 by using sepharose-4B-l tyrosine-sulfanilamide affinity gel chromatography. The molecular weight determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was found to be about 29.9 kDa. The kinetic parameters, K-M and V-max were determined for the 4-nitrophenyl acetate hydrolysis reaction. Some sulfonamides were tested as inhibitors against the purified CA enzymes. The K-i constants for mafenide (1), p-toluenesulfonamide (2), 2-bromo-benzene sulfonamide (3), 4-chlorobenzene sulfonamide (4), 4-amino-6-chloro-1-3 benzenedisulfonamide (5), sulfamethazine (6), sulfaguanidine (7), sulfadiazine (8), and acetozazolamide (9) were in the range of 7.5-108.75 M. (C) 2014 Wiley Periodicals, Inc.