Hg2+-mediated stabilization of G-triplex based molecular beacon for label-free fluorescence detection of Hg2+, reduced glutathione, and glutathione reductase activity

Author(s):  
Rong-Mei Kong ◽  
Lin Ma ◽  
Xue Han ◽  
Chunran Ma ◽  
Fengli Qu ◽  
...  
1978 ◽  
Vol 174 (3) ◽  
pp. 819-825 ◽  
Author(s):  
E C Abraham ◽  
J F Taylor ◽  
C A Lang

In order to determine whether the biological age of a mouse influences erythrocyte metabolism and erythrocyte aging in vivo, blood samples were collected from male C57/BL6J mice of different biological ages ranging from mature (10 months) to “very old” (37 months). In the very old mouse, compared with the mature mouse, the erythrocyte survival time was decreased, erythrocyte densities were increased, the concentrations of total free thiol and reduced glutathione, and glutathione reductase activity were decreased. Erythrocytes were separated into different density (age) groups by phthalate ester two-phase centrifugation or by albumin density-gradient centrifugation. The density-age relationship of erythrocytes was established by pulse-labelling with 59Fe in vivo and by subsequent determinations of specific radioactivity of erythrocyte fractions of different densities prepared during a chase period of 60 days. The age of erythrocytes in mice of all ages was directly related to density. Also, in older erythrocytes compared with younger erythrocytes, decreased concentrations of total free thiol and reduced glutathione, and decreased glutathione reductase activity were observed. These were the lowest in the old erythrocytes of very old mice. These results in aging erythrocytes from aging mice suggest that the glutathione status the erythrocyte may be an index of aging, not only of the cell but also of the organism.


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.


1964 ◽  
Vol 10 (1) ◽  
pp. 53-61
Author(s):  
Hugo R Rony ◽  
Michael West ◽  
Hyman J Zimmerman

Abstract Studies of serum glutathione reductase activity in this laboratory prompted an attempt to demonstrate glutathione oxidase in the serum. The oxidation of reduced glutathione in the sera of patients with various diseases does not differ from normal sera. Preheating the serum and addition of cytochrome c does not effect the oxidizing capacity of the serum. The ability of serum to oxidize reduced glutathione appears to represent autoxidation, not the effect of an oxidizing enzyme.


1955 ◽  
Vol 33 (1) ◽  
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.


1990 ◽  
Vol 45 (1-2) ◽  
pp. 96-106 ◽  
Author(s):  
Samuel P. Yenne ◽  
Kriton K. Hatzios

The influence of the oxime ether safeners, oxabetrinil and CGA-133205, on glutathione content, glutathione reductase (EC 1.6.4.2), and glutathione-S-transferase (EC 2.5.1.18) activity in seeds and seedlings of grain sorghum (Sorghum bicolor (L.) Moench. var. Funk G-522-DR) was investigated. Plant material for these experiments was derived from seed that was either untreated, or treated with 1.25 or 0.4g ai/kg seed of oxabetrinil or CGA-133205, respectively. Measurements were conducted at 0, 1, 2, 4, 8 , 12, 24, 36, and 72 h after the initiation of germination. In safener-treated sorghum seeds, the levels of total and reduced glutathione decreased gradually after the initiation of germination reaching a low at 8 to 12 h and then increased continuously reaching a maximum at 48 h. The greatest increases in glutathione levels were observed in oxabetrinil-treated sorghum seedlings. Glutathione reductase activity was consistently higher in untreated seeds of grain sorghum for the first 24 h of imbibition, but at 36 to 72 h glutathione reductase activity increased in the safener-treated tissues. CGA-133205 appeared to have a greater stimulatory influence on the activity of glutathione reductase than did oxabetrinil. For the first 8 h after germination was initiated, glutathione-S-transferase activity in oxabetrinil- and CGA-133205-treated seeds remained enhanced compared to that of untreated seeds, but was at or below the levels of the activity of glutathione-S-transferase extracted from untreated seeds for the remainder of the experiment. Non-enzymatic conjugation of metolachlor with reduced glutathione increased as the pH of the reaction solution increased from 6.0 to 8.0. Oxabetrinil at 1 to 40 μM and CGA-133205 at 1 to 160 μm enhanced nonenzymatic conjugation of m etolachlor with glutathione. At 80 and 160 |j.m , oxabetrinil reduced the am oun t of non-enzym atic conjugation of metolachlor. Oxabetrinil conjugated with reduced glutathione at low rates either enzymatically or non-enzymatically at pH 8.0 while CGA-133205 did not at any pH. In the presence of metolachlor, the amount of non-enzymatic conjugation of oxabetrinil was decreased, indicating that metolachlor is more reactive towards glutathione than is oxabetrinil. Overall, these data suggest that during the early stages of seed germination and seedling development of grain sorghum , oxim e ether safeners can enhance the detoxication of the herbicide, metolachlor, through enzymatic or non-enzymatic conjugation to reduced glutathione by enhancing either the level of reduced glutathione and/or the activity of glutathione-related enzymes.


Author(s):  
G. Albrecht ◽  
E.-M. Wiedenroth

SynopsisDuring the first 2 h of oxygen re-exposure, the GSH level was almost constant, while the GSSG increased about 10-fold. This results in a decline of the GSH/GSSG ratio, which reflects oxidative stress induced by re-aeration following hypoxic pretreatment. Further evidence for this is an increase in lipid peroxidation measured as thiobarbituric acid-reactive material (TBA-rm) and the affected content of sulfydryl-groups in the root tissues.In spite of the high level of reduced glutathione in the roots under hypoxia-inducing conditions, they contained a retarded glutathione reductase (GR) activity compared with aerobically grown roots. Re-aeration up to 2 h resulted in a further decrease in GR activity. Only at the end of the 16-h period of re-aeration the enzyme activity was able to recover, by overshooting slightly those values of the continuously aerated controls. This was accompanied by a restoring a high GSH/GSSG ratio and an enhanced level of GSH.


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