Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1237006 | Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy | 2005 | 5 Pages |
Abstract
A highly sensitive spectrofluorimetric method for the determination of reduced glutathione (GSH,γ-l-glutamyl-l-cysteinylglycine) based on its inhibitory effect on hemoglobin activity was developed. Multienzyme redox system is the most important biological oxidation process in cellular respiration chain. Under the action of hemoglobin, NADH can be oxidized by hydrogen peroxide (H2O2) to form a dimmer that is optimally fluorescent. Under the optimum conditions, the degree of inhibitory effect was linear to the GSH concentration in the range of 5.00 Ã 10â8 to 9.60 Ã 10â6 mol lâ1. The relative standard deviation was 3.70% for 11 determinations of 5.00 Ã 10â6 mol lâ1 GSH and the detection limit was 8.00 Ã 10â9 mol lâ1. Further experimental results revealed that the inhibition of GSH on this system was of the competitive type.
Keywords
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Chen Yahong, Cai Ruxiu,