Merck
  • Home
  • Search Results
  • Characterization and inhibition studies of an α-carbonic anhydrase from the endangered sturgeon species Acipenser gueldenstaedti.

Characterization and inhibition studies of an α-carbonic anhydrase from the endangered sturgeon species Acipenser gueldenstaedti.

Journal of enzyme inhibition and medicinal chemistry (2011-03-09)
Sevgi Kolayli, Fatma Karahalil, Huseyin Sahin, Barbaros Dincer, Claudiu T Supuran
ABSTRACT

An α-carbonic anhydrase (CA, EC 4.2.1.1) was purified and characterized kinetically from erythrocytes of the sturgeon Acipenser gueldenstaedti, an endangered species. The sturgeon enzyme (AgCA) showed kinetic parameters for the CO(2) hydration reaction comparable with those of the human erythrocytes enzyme hCA II, being a highly active enzyme, whereas its esterase activity with 4-nitrophenyl acetate as substrate was lower. Sulphonamide inhibitors (acetazolamide, sulphanilamide) strongly inhibited AgCA, whereas metal ions (Ag(+), Zn(2+), Cu(2+) and Co(2+)) were weak, millimolar inhibitors. Several widely used pesticides (2,4-dichlorophenol, dithiocarbamates, parathion and carbaryl) were also assayed as inhibitors of this enzyme. The dithiocarbamates were low micromolar AgCA inhibitors (IC(50) of 16-18 μM), whereas the other pesticides inhibited the enzyme with IC(50)s in the range of 102-398 μM. The wide use of dithiocarbamate pesticides may be one of the factors enhancing the vulnerability of this sturgeon species to pollutants.

MATERIALS
Product Number
Brand
Product Description

Supelco
Sulfanilamide melting point standard, Pharmaceutical Secondary Standard; Certified Reference Material
Sigma-Aldrich
Sulfanilamide, puriss. p.a., ≥99% (calc. to the dried substance)
Supelco
Sulfanilamide, VETRANAL®, analytical standard
Sigma-Aldrich
Sulfanilamide, ≥98%
Sigma-Aldrich
Sulfanilamide, Vetec, reagent grade, 97%