Intracellular mechanisms for the decomposition of a lipid peroxide. II. Decomposition of a lipid peroxide by subcellular fractions

1969 ◽  
Vol 47 (5) ◽  
pp. 493-499 ◽  
Author(s):  
P. J. O'Brien ◽  
C. Little

The properties of subcellular fractions of rat liver in catalyzing the decomposition of linoleic acid hydroperoxide have been compared with those of transition salts, heme compounds, and nucleophiles. The properties compared included the range of products produced, the pH dependence of the reaction, and the effects of metal-complexing agents, inhibitors, and hydrogen donors. It was concluded that the decomposition of the hydroperoxide in the liver cell was due principally to reaction with the intracellular nucleophile glutathione by a mechanism catalyzed by the enzyme glutathione peroxidase. In the absence of glutathione, however, both the mitochondrial and microsomal fractions decomposed the hydroperoxide presumably by a radical mechanism probably involving the cytochromes.

1969 ◽  
Vol 47 (5) ◽  
pp. 485-492 ◽  
Author(s):  
P. J. O'Brien

Linoleic acid hydroperoxide was prepared. Two types of mechanisms for its decomposition were found. The hydroperoxide was rapidly decomposed by certain transition metal ions, heme, and hemoprotein to a complex range of products, the decomposition being accompanied by changes in ultraviolet absorption spectra. The production of radical oxidizing species may account for these products. It was also found that the hydroperoxide could be decomposed by nucleophiles presumably in a nonradical reaction to a hydroxy acid without any change in ultraviolet spectra.The kinetics, the pH dependence, and the effects of metal-complexing agents, inhibitors, and hydrogen donors on the catalytic activity of the metal ions and heme compounds were also investigated.


1980 ◽  
Vol 58 (10) ◽  
pp. 1012-1017 ◽  
Author(s):  
Paul Morrissey ◽  
Peter J. O'Brien

The reduction of linoleic acid hydroperoxide catalyzed by rat liver cytosol was previously shown to be catalyzed by a selenium-dependent glutathione peroxidase. In contrast, the activity in rabbit liver cytosol could also be attributed to a selenium-independent glutathione peroxidase present in an approximately equal amount to the selenium-dependent peroxidase. The selenium-independent peroxidase copurified with glutathione transferase B and was completely inhibited by antitransferase B antiserum and transferase substrates. These results suggest that glutathione transferase B in rabbit liver cytosol is involved in the intracellular decomposition of lipid peroxide and could explain the lower selenium requirement of rabbits in comparison with other species.


1979 ◽  
Vol 177 (2) ◽  
pp. 761-763 ◽  
Author(s):  
M R Shreve ◽  
P G Morrissey ◽  
P J O'Brien

The reduction of linoleic acid hydroperoxide catalysed by rat liver cytosol was previously shown to be catalysed by a selenium-dependent glutathione peroxidase. In contrast, the enzyme responsible in guinea-pig liver cytosol is not selenium-dependent and appears to be a glutathione transferase.


1990 ◽  
Vol 54 (12) ◽  
pp. 3289-3293 ◽  
Author(s):  
Yoshiharu INOUE ◽  
Takayuki ICHIRYU ◽  
Koji YOSHIKAWA ◽  
Linh-Thuoc TRAN ◽  
Kousaku MURATA ◽  
...  

1990 ◽  
Vol 54 (12) ◽  
pp. 3289-3293
Author(s):  
Yoshiharu Inoue ◽  
Takayuki Ichiryu ◽  
Koji Yoshikawa ◽  
Linh-Thuoc Tran ◽  
Kousaku Murata ◽  
...  

1982 ◽  
Vol 69 (6) ◽  
pp. 1308-1314 ◽  
Author(s):  
Jacques Dupont ◽  
Pierre Rustin ◽  
Claude Lance

2002 ◽  
Vol 25 (8) ◽  
pp. 1093-1096 ◽  
Author(s):  
Naoko Sasaki ◽  
Takeshi Toda ◽  
Takao Kaneko ◽  
Naomichi Baba ◽  
Mitsuyoshi Matsuo

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