Amperometric determination of reduced glutathione with a new Co-based metal-organic coordination polymer modified electrode

2014 ◽  
Vol 40 ◽  
pp. 92-95 ◽  
Author(s):  
Baiqing Yuan ◽  
Renchun Zhang ◽  
Xixi Jiao ◽  
Juan Li ◽  
Huaizhong Shi ◽  
...  
2009 ◽  
Vol 21 (12) ◽  
pp. 1348-1353 ◽  
Author(s):  
Goretti Díaz-Díaz ◽  
M. Carmen Blanco-López ◽  
M. Jesús Lobo-Castañón ◽  
Arturo J. Miranda-Ordieres ◽  
Paulino Tuñón-Blanco

2000 ◽  
Vol 2 (11) ◽  
pp. 782-785 ◽  
Author(s):  
Jyh-Myng Zen ◽  
Dong-Mung Tsai ◽  
Annamalai Senthil Kumar ◽  
Venkataraman Dharuman

1955 ◽  
Vol 33 (3) ◽  
pp. 404-407 ◽  
Author(s):  
H. Bruce Collier ◽  
Sheila C. McRae

Glutathione reductase activity of hemolyzates of human erythrocytes was measured by an amperometric titration of the reduced glutathione that is formed from oxidized glutathione. The electron donor in the system was reduced triphosphopyridine nucleotide, produced by the glucose-6-phosphate dehydrogenase of the cells. Removal of the red-cell stromata from hemolyzates slightly increased the reductase activity. Addition of Na+, K+, or Ca++ had no effect on the enzyme. No marked inhibition was observed in the presence of phenothiazine, phenothiazone, phenylhydrazine, or p-chloromercuribenzoate.


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