Purification and characterization of carbonic anhydrase from Ağrı Balık Lake trout gill (Salmo trutta labrax) and effects of sulfonamides on enzyme activity.

Abstract:

:Carbonic anhydrase (CA) was purified from Ağrı Balık 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 Ki 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 μM.

journal_name

J Biochem Mol Toxicol

authors

Demirdag R,Comakli V,Kuzu M,Yerlikaya E,Şentürk M

doi

10.1002/jbt.21675

subject

Has Abstract

pub_date

2015-03-01 00:00:00

pages

123-8

issue

3

eissn

1095-6670

issn

1099-0461

journal_volume

29

pub_type

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