Characterization and inhibition studies of carbonic anhydrase from gill of Russian Sturgeon Fish (Acipenser gueldenstaedtii).
Identifieur interne : 000096 ( Main/Exploration ); précédent : 000095; suivant : 000097Characterization and inhibition studies of carbonic anhydrase from gill of Russian Sturgeon Fish (Acipenser gueldenstaedtii).
Auteurs : Barbaros Dinçer ; Arife P Nar Ekinci ; Gülay Akyüz ; Lker Zeki Kurto Lu [Turquie]Source :
- Journal of enzyme inhibition and medicinal chemistry [ 1475-6374 ] ; 2016.
Abstract
An α-carbonic anhydrase (CA, EC 4.2.1.1) was purified and characterized kinetically from gill of Acipenser gueldenstaedtii as an endangered sturgeon species. The carbonic anhydrase was purified 66-folds with yield 20.7% by Sepharose-4B-l-tyrosine-sulfanilamide affinity column and the specific activity was determined as 222.2 EU/mg protein. Km and Vmax kinetic values for gill carbonic anhydrase were calculated by a Lineweaver-Burk graph using p-nitrophenol acetate (p-NPA) as a substrate, and was defined as 2.5 mM and 5 × 10(6 )μM/min, respectively. It was observed that CA from the sturgeon gill in the presence of the sulfanilamide and acetazolamide as an inhibitor had very low IC50 values such as 13.0 and 0.1 μM, respectively. In addition, it was determined that the enzyme was inhibited by Fe(2+,) Co(2+,) Ni(2+), and Zn(2+)-Ba(2+) with the IC50 values of 0.2, 1.7, 1.2, and 1.1 mM, respectively.
DOI: 10.3109/14756366.2015.1076810
PubMed: 26290152
Affiliations:
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type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">An α-carbonic anhydrase (CA, EC 4.2.1.1) was purified and characterized kinetically from gill of Acipenser gueldenstaedtii as an endangered sturgeon species. The carbonic anhydrase was purified 66-folds with yield 20.7% by Sepharose-4B-l-tyrosine-sulfanilamide affinity column and the specific activity was determined as 222.2 EU/mg protein. Km and Vmax kinetic values for gill carbonic anhydrase were calculated by a Lineweaver-Burk graph using p-nitrophenol acetate (p-NPA) as a substrate, and was defined as 2.5 mM and 5 × 10(6 )μM/min, respectively. It was observed that CA from the sturgeon gill in the presence of the sulfanilamide and acetazolamide as an inhibitor had very low IC50 values such as 13.0 and 0.1 μM, respectively. In addition, it was determined that the enzyme was inhibited by Fe(2+,) Co(2+,) Ni(2+), and Zn(2+)-Ba(2+) with the IC50 values of 0.2, 1.7, 1.2, and 1.1 mM, respectively.</div></front></TEI><affiliations><list><country><li>Turquie</li></country></list><tree><noCountry><name sortKey="Akyuz, Gulay" sort="Akyuz, Gulay" uniqKey="Akyuz G" first="Gülay" last="Akyüz">Gülay Akyüz</name><name sortKey="Dincer, Barbaros" sort="Dincer, Barbaros" uniqKey="Dincer B" first="Barbaros" last="Dinçer">Barbaros Dinçer</name><name sortKey="Ekinci, Arife P Nar" sort="Ekinci, Arife P Nar" uniqKey="Ekinci A" first="Arife P Nar" last="Ekinci">Arife P Nar Ekinci</name></noCountry><country name="Turquie"><noRegion><name sortKey="Kurto Lu, Lker Zeki" sort="Kurto Lu, Lker Zeki" uniqKey="Kurto Lu " first=" Lker Zeki" last="Kurto Lu"> Lker Zeki Kurto Lu</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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