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Inhibitory effects of flavonoids on aldehyde oxidase activity.
Pirouzpanah, Saeed; Hanaee, Jalal; Razavieh, Seyed-Vali; Rashidi, Mohammad-Reza.
Afiliação
  • Pirouzpanah S; School of Health and Nutrition, Tabriz University of Medical Sciences, Tabriz, Iran.
J Enzyme Inhib Med Chem ; 24(1): 14-21, 2009 Feb.
Article em En | MEDLINE | ID: mdl-18608746
Flavonoids are an important group of natural compounds that can interfere with the activity of some enzymes. In this study, effects of various flavonoids on aldehyde oxidase (AO) activity were evaluated in vitro. AO was partially purified from guinea pig liver. The effects of 12 flavonoids from three subclasses of flavon-3-ol, flavan-3-ol and flavanone on the oxidation of vanillin and phenanthridine as substrates of AO and xanthine as a substrate of xanthine oxidase (XO) were investigated spectrophotometrically. Among the 12 flavonoids, myricetin and quercetin were the most potent inhibitors of both AO and XO. In general, the oxidation of vanillin was more inhibited by flavonoids than that of phenanthridine. Almost all of the flavonoids inhibited AO activity more potently than XO, which was more evident with non-planner flavanols. A planner structure seems to be essential for a potent inhibitory effect and any substitution by sugar moieties reduces the inhibitory effects. This study could provide a new insight into AO natural inhibitors with potential to lead to some food-drug interactions.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Flavonoides / Aldeído Oxidase Limite: Animals Idioma: En Revista: J Enzyme Inhib Med Chem Assunto da revista: BIOQUIMICA / QUIMICA Ano de publicação: 2009 Tipo de documento: Article País de afiliação: Irã País de publicação: Reino Unido

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Flavonoides / Aldeído Oxidase Limite: Animals Idioma: En Revista: J Enzyme Inhib Med Chem Assunto da revista: BIOQUIMICA / QUIMICA Ano de publicação: 2009 Tipo de documento: Article País de afiliação: Irã País de publicação: Reino Unido