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1.
J Enzyme Inhib Med Chem ; 30(3): 479-83, 2015 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-25198891

RESUMO

Lactoperoxidase (LPO) catalyzes the oxidation of numerous of organic and inorganic substrates by hydrogen peroxide. It has very vital activity in the innate immune system by decreasing or stopping the activation of the bacteria in milk and mucosal secretions. This study's purpose was to investigate in vitro effect of some phenolic acids (ellagic, gallic, ferulic, caffeic, quercetin, p-coumaric, syringic, catechol and epicatechin) on the purified LPO. This enzyme was purified from milk by using different methods such as Amberlite CG-50 resin, CM-Sephadex C-50 ion-exchange and Sephadex G-100 gel filtration chromatography. LPO was purified 28.7-fold with a yield of 20.03%. We found phenolic acids have inhibition effects on bovine LPO enzyme to different concentrations. Our study showed lower concentrations of caffeic acid, ferulic acid and quercetin exhibited much higher inhibitory effect on enzyme, so these three of them were clearly a more potent inhibitor than the others were. All of compounds were non-competitive inhibitors.


Assuntos
Hidroxibenzoatos/farmacologia , Lactoperoxidase/antagonistas & inibidores , Animais , Bovinos , Relação Dose-Resposta a Droga , Hidroxibenzoatos/química , Lactoperoxidase/metabolismo , Estrutura Molecular , Relação Estrutura-Atividade
2.
Chem Biol Drug Des ; 75(5): 515-20, 2010 May.
Artigo em Inglês | MEDLINE | ID: mdl-20486938

RESUMO

The inhibitory effects of some phenolic acids on the cytosolic human carbonic anhydrase (hCA, EC 4.2.1.1) isozymes hCA I and hCA II were investigated. Ellagic acid, gallic acid, ferulic acid, caffeic acid, quercetin, p-coumaric acid, p-hydroxybenzoic acid, and syringic acid showed K(I) values in the range of 99-1061 microm for hCA I and of 105-758 microm against hCA II, respectively. Quercetin (for hCA I), p-coumaric acid (for hCA II), and gallic acid (for hCA II) exhibited competitive inhibitory effects with 4-nitrophenyl acetate as substrate. All of the other phenolic acids were found as non-competitive inhibitors with 4-nitrophenylacetate as substrate for hCA I and hCA II. The phenolic acids investigated here showed thus interesting hCA I and hCA II inhibitory effects and might be used as leads for generating enzyme inhibitors possibly targeting other CA isoforms which have not been yet assayed for their interactions with such agents.


Assuntos
Anidrase Carbônica II/antagonistas & inibidores , Anidrase Carbônica I/antagonistas & inibidores , Inibidores da Anidrase Carbônica/química , Eritrócitos/enzimologia , Hidroxibenzoatos/química , Anidrase Carbônica I/metabolismo , Anidrase Carbônica II/metabolismo , Inibidores da Anidrase Carbônica/farmacologia , Humanos , Hidroxibenzoatos/farmacologia , Cinética
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