ZX-33104-96 | Glutathione Reductase (GR) Activity Assay (Fluorometric)
Glutathione reductase (GR) also known as glutathione-disulfide reductase (GSR) is an enzyme that plays an indirect but essential role in prevention of cellular oxidative damage by helping to maintain appropriate levels of intracellular glutathione (GSH). GSH, in conjuction with the enzyme glutathione peroxidase (GP), is the acting reductant responsible for minimizing harmful hydrogen peroxide cellular levels. The regeneration of GSH is catalyzed by GSR. GSR is a ubiquitous 100-120 kDa dimeric flavoprotein that catalyzes the reduction of oxidized glutathione (GSSG) to reduced glutathione, using β-nicotinamide dinucleotide phosphate (NADPH) as the hydrogen donor. Molecules such as NADPH act as hydride donors in a variety of enzymatic processes. NADPH has been suggested to also act as an indirectly operating antioxidant, given its role in the re-reduction of GSSG to GSH and thus maintaining the antioxidative power of glutathione.
The most widely used procedure to measure GR is to monitor the oxidation of NADPH as a decrease in absorbance at 340 nm. However this method suffers from the absorbance of many biological molecules at 340 nm. The Glutathione Reductase (GR) Activity Assay determines GSR activity by directly measuring the amount of GSH generated from the reduction of GSSG by reacting the GSH with a non-fluorescent molecule, Fluorescent Detection Reagent, to covalently bind the free thiol group on GSH and yield a highly fluorescent product.
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