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Characterization and anions inhibition studies of an α-carbonic anhydrase from the teleost fish Dicentrarchus labrax.

Abstract：

:Carbonic anhydrase (CA; EC 4.2.1.1) was purified from the gill of the teleost fish Dicentrarchus labrax (European seabass). The purification procedure consisted of a single step affinity chromatography on Sepharose 4B-tyrosine-sulfanilamide. The enzyme was purified 84.9-fold with a yield of 58%, and a specific activity of 838.9 U/mg proteins. It has an optimum pH at 8.0; an optimum temperature at 10°C. The kinetic parameters of this enzyme were determined for its esterase activity, with 4-nitrophenyl acetate (NPA) as substrate. The following anions, H₂NSO₃⁻, I⁻, SCN⁻, NO₃⁻, NO₂⁻, N₃⁻, Br⁻, Cl⁻, SO₄²⁻, and F⁻ showed inhibitory effects on the enzyme. Sulfamic acid, iodide, and thiocyanate exhibited the strongest inhibitory action, in the micromolar range (K(i)s of 87-187 μM). NO₃⁻, NO₂⁻ and N₃⁻ were moderate inhibitors, whereas other anions showed only weak actions. All tested anions inhibited the enzyme in a competitive manner. Our findings indicate that these anions inhibit the fish enzyme in a similar manner to other α-CAs from mammals investigated earlier, but the susceptibility to various anions differs significantly between the fish and mammalian CAs.

journal_name

Bioorg Med Chem

journal_title

Bioorganic & medicinal chemistry

authors

Ekinci D,Ceyhun SB,Sentürk M,Erdem D,Küfrevioğlu Oİ,Supuran CT

doi

10.1016/j.bmc.2010.12.033

subject

Has Abstract

pub_date

2011-01-15 00:00:00

pages

744-8

issue

2

eissn

0968-0896

issn

1464-3391

pii

S0968-0896(10)01124-7

journal_volume

19

pub_type

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