scholarly journals Oxidation of Glutathione and Other Thiols by the Xanthine Oxidase and Hypoxanthine of Rat Liver Homogenates

Nature ◽  
1964 ◽  
Vol 202 (4937) ◽  
pp. 1115-1115 ◽  
Author(s):  
P. C. JOCELYN
1953 ◽  
Vol 200 (1) ◽  
pp. 303-310
Author(s):  
G. Litwack ◽  
J.W. Bothwell ◽  
J.N. Williams ◽  
C.A. Elvehjem

1970 ◽  
Vol 117 (5) ◽  
pp. 947-949 ◽  
Author(s):  
P. C. Jocelyn

1. The aerobic oxidation of GSH and other thiols by rat liver homogenate is abolished either by previous dialysis or by removal of the proteins but is restored by a mixture of the protein-free filtrate and the dialysed homogenate. 2. The oxidation is prevented by previously heating the dialysed homogenate but not the protein-free filtrate and also by known inhibitors of xanthine oxidase. 3. A similar oxidation occurs with hypoxanthine in place of of protein-free filtrate.


1968 ◽  
Vol 46 (9) ◽  
pp. 1047-1056
Author(s):  
D. G. R. Blair ◽  
B. D. McLennan

The xanthine oxidase activity of rat liver homogenates increased severalfold when the homogenates were stored (aged) at 4 °C for several days. The increase could be demonstrated by measuring xanthine oxidase activity by xanthine utilization or allantoin formation from xanthine. The increase in activity was not correlated with the concentrations of allantoin, uric acid, xanthine, or hypoxanthine in the homogenates, and, therefore, is not attributed to decrease of substrate inhibition, but its demonstration was partially inhibited by relatively high concentrations of xanthine in the enzyme-assay reaction medium.The increase in xanthine oxidase activity was temperature-dependent and was unaffected by the presence of glucose or adenosine 5′-triphosphate. Lysis of unbroken cells during the aging period and microbial contamination were not contributory. Dialysis of a fresh homogenate partially inhibited the increase in activity, but the addition of the dialysate of an aging homogenate to a dialyzed or fresh homogenate did not stimulate activity.The mechanism of the increase in xanthine oxidase activity has not been elucidated, but the fact that stimulation of the activity by methylene blue decreases as the homogenates age, suggests that the rate at which reduced xanthine oxidase is oxidized by air may increase with homogenate aging.


1949 ◽  
Vol 181 (1) ◽  
pp. 255-271 ◽  
Author(s):  
Dan A. Richert ◽  
Sally. Edwards ◽  
W.W. Westerfeld

1954 ◽  
Vol 206 (1) ◽  
pp. 471-481 ◽  
Author(s):  
Ivan D. Frantz ◽  
Nancy L.R. Bucher ◽  
Henny S. Schneider ◽  
Naomi H. McGovern ◽  
Ruth Kingston

1957 ◽  
Vol 225 (2) ◽  
pp. 735-744
Author(s):  
Henry Kamin ◽  
Mildred A. Koon ◽  
Philip Handler
Keyword(s):  

1962 ◽  
Vol 202 (2) ◽  
pp. 343-346 ◽  
Author(s):  
Dennis D. Goetsch ◽  
L. E. McDonald

The effects of glucocorticoid administration on oxygen uptake, glucose and glycogen disappearance, lactic acid formation, and inorganic phosphate and protein levels in rat liver homogenates have been studied. A single injection of hydrocortisone, prednisolone, or 9 α-fluoroprednisolone 5 hr before sacrifice resulted in a highly significant increase in oxygen uptake by rat liver homogenates, whereas chronic administration of prednisolone daily for 7 days caused a marked inhibition in homogenate respiration. Glycolytic rate did not appear to be affected by single injections since endogenous carbohydrate utilization was similar in liver homogenates prepared from control and treated animals. Incubation of liver homogenates under aerobic conditions disclosed that inorganic phosphate levels were decreased in homogenates from corticoid-treated rats, whereas these levels were similar in treated and control liver homogenates incubated under nitrogen. Under anaerobic conditions, liver homogenates from treated rats accumulated lactic acid more rapidly than untreated liver homogenates. Glucocorticoid treatment did not appear to affect protein disappearance since no differences between protein levels in treated and untreated rat liver homogenates were detected following incubation.


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