In vitro effects of rosmarinic acid on glutathione reductase and glucose 6-phosphate dehydrogenase

TANDOGAN B., KURUUZUM-UZ A., SENGEZER C., GÜVENALP Z., DEMİREZER L. Ö., ULUSU N. N.

PHARMACEUTICAL BIOLOGY, vol.49, no.6, pp.587-594, 2011 (SCI-Expanded) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 49 Issue: 6
  • Publication Date: 2011
  • Doi Number: 10.3109/13880209.2010.533187
  • Journal Name: PHARMACEUTICAL BIOLOGY
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.587-594
  • Keywords: Enzyme inhibition, kinetics, natural product, purification, NATURAL PHENOLIC-COMPOUNDS, PURIFICATION, BINDING, KIDNEY, ANTIOXIDANT, DERIVATIVES, MECHANISM, SUBSTRATE, KINETICS, AMYLASE
  • Hacettepe University Affiliated: Yes

Abstract

Context: Glutathione reductase (GR, NADPH:oxidized glutathione oxidoreductase, E. C 1.6.4.2) is a flavoprotein that catalyzes the NADPH-dependent reduction of oxidized glutathione (GSSG). GR is a crucial enzyme in the antioxidant system by maintaining reduced glutathione (GSH). Glucose 6-phosphate dehydrogenase (G6PD, glucose 6-phosphate (G6P):NADP(+) oxidoreductase, EC 1.1.1.49) is the key regulatory enzyme of the pentose phosphate pathway and maintains NADPH for reductive reactions.