scholarly journals Lipid and steroid hydroperoxides as substrates for the non-selenium-dependent glutathione peroxidase

1979 ◽  
Vol 177 (2) ◽  
pp. 761-763 ◽  
Author(s):  
M R Shreve ◽  
P G Morrissey ◽  
P J O'Brien
Keyword(s):  
Linoleic Acid ◽  
Glutathione Peroxidase ◽  
Guinea Pig ◽  
Glutathione Transferase ◽  
Linoleic Acid Hydroperoxide ◽  
Pig Liver ◽  
Liver Cytosol ◽  
Acid Hydroperoxide ◽  
Guinea Pig Liver ◽  
Rat Liver Cytosol

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.

Selenium-independent glutathione peroxidase activity in rabbit liver

1980 ◽  
Vol 58 (10) ◽  
pp. 1012-1017 ◽  
Author(s):  
Paul Morrissey ◽  
Peter J. O'Brien
Keyword(s):  
Linoleic Acid ◽  
Glutathione Peroxidase ◽  
Glutathione Transferase ◽  
Lipid Peroxide ◽  
Rabbit Liver ◽  
Linoleic Acid Hydroperoxide ◽  
Glutathione Peroxidase Activity ◽  
Liver Cytosol ◽  
Acid Hydroperoxide ◽  
Rat Liver Cytosol

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.

Glutathione peroxidase II of guinea pig liver cytosol: Relationship to glutathione S-transferases

1980 ◽  
Vol 205 (1) ◽  
pp. 122-131 ◽  
Author(s):  
Carl Irwin ◽  
Judy K. O'Brien ◽  
Peter Chu ◽  
Janis K. Townsend-Parchman ◽  
Pat O'Hara ◽  
...  
Keyword(s):  
Glutathione Peroxidase ◽  
Guinea Pig ◽  
Pig Liver ◽  
Liver Cytosol ◽  
Glutathione S Transferases ◽  
Guinea Pig Liver ◽  
Glutathione Peroxidase Ii

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
Keyword(s):  
Linoleic Acid ◽  
Glutathione Peroxidase ◽  
Ph Dependence ◽  
Lipid Peroxide ◽  
Subcellular Fractions ◽  
Radical Mechanism ◽  
Complexing Agents ◽  
Linoleic Acid Hydroperoxide ◽  
Hydrogen Donors ◽  
Acid Hydroperoxide

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.

(S)-Preferential detoxification of 4-hydroxy-2(E)-nonenal enantiomers by hepatic glutathione S-transferase isoforms in guinea-pigs and rats

2001 ◽  
Vol 355 (1) ◽  
pp. 237-244 ◽  
Author(s):  
Akira HIRATSUKA ◽  
Kouichi TOBITA ◽  
Hiroshi SAITO ◽  
Yasuhiro SAKAMOTO ◽  
Hiroaki NAKANO ◽  
...  
Keyword(s):  
Guinea Pig ◽  
Guinea Pigs ◽  
High Catalytic Activity ◽  
Glutathione S Transferase ◽  
Pig Liver ◽  
Liver Cytosol ◽  
Glutathione S Transferases ◽  
Human Livers ◽  
A Minor ◽  
Guinea Pig Liver

In guinea-pig liver cytosol, racemic 4-hydroxy-2(E)-nonenal (HNE), a reactive and highly toxic product released from biomembranes by lipid peroxidation, was detoxified (S)-preferentially by GSH conjugation mediated by glutathione S-transferases (GSTs) and (R)-preferentially by NAD+-dependent oxidation mediated by aldehyde dehydrogenase (ALDH). The GST-mediated detoxification of the HNE enantiomers proceeded at much higher rates than that mediated by ALDH in guinea-pig liver cytosol. All the major guinea-pig GSTs, A1-1, M1-1, M1-2 and M1-3*, isolated from guinea-pig liver cytosol also catalysed the (S)-preferential conjugation of the HNE enantiomers. The liver and other major tissues of guinea-pigs had no immunologically detectable level of a putative GSTA4-4 orthologue, which exists as a minor GST protein in rat, mouse and human livers and exhibits extremely high catalytic activity towards HNE. All the hepatic rat GSTs, A1-1(2), A1-3, A4-4, M1-1, M1-2 and M2-2, also catalysed the (S)-preferential conjugation of HNE enantiomers.

scholarly journals Guinea-pig liver testosterone 17 β-dehydrogenase (NADP+) and aldehyde reductase exhibit benzene dihydrodiol dehydrogenase activity

1985 ◽  
Vol 225 (1) ◽  
pp. 177-181 ◽  
Author(s):  
A Hara ◽  
M Hayashibara ◽  
T Nakayama ◽  
K Hasebe ◽  
S Usui ◽  
...  
Keyword(s):  
Guinea Pig ◽  
Dehydrogenase Activity ◽  
Aldehyde Reductase ◽  
Pig Liver ◽  
Liver Cytosol ◽  
Dihydrodiol Dehydrogenase ◽  
Guinea Pig Liver ◽  
Oxidation Of Benzene

We have kinetically and immunologically demonstrated that testosterone 17 beta-dehydrogenase (NADP+) isoenzymes (EC 1.1.1.64) and aldehyde reductase (EC 1.1.1.2) from guinea-pig liver catalyse the oxidation of benzene dihydrodiol (trans-1,2-dihydroxycyclohexa-3,5-diene) to catechol. One isoenzyme of testosterone 17 beta-dehydrogenase, which has specificity for 5 beta-androstanes, oxidized benzene dihydrodiol at a 3-fold higher rate than 5 beta-dihydrotestosterone, and showed a more than 4-fold higher affinity for benzene dihydrodiol and Vmax. value than did another isoenzyme, which exhibits specificity for 5 alpha-androstanes, and aldehyde reductase. Immunoprecipitation of guinea-pig liver cytosol with antisera against the testosterone 17 beta-dehydrogenase isoenzymes and aldehyde reductase indicated that most of the benzene dihydrodiol dehydrogenase activity in the tissue is due to testosterone 17 beta-dehydrogenase.

Phosphatidylinositol movement between isolated microsomal and mitochondrial membranes

1983 ◽  
Vol 61 (12) ◽  
pp. 1282-1291 ◽  
Author(s):  
J. Chudzik ◽  
N. Z. Stanacev
Keyword(s):  
Guinea Pig ◽  
Direct Contact ◽  
Reaction Medium ◽  
Mitochondrial Membranes ◽  
Pig Liver ◽  
Liver Cytosol ◽  
Microsomal Membranes ◽  
Membrane Bound ◽  
Phosphatidylinositol Transfer ◽  
Guinea Pig Liver

Transfer of membrane-bound phosphatidyl-[2′-3H]inositol from microsomal to unlabelled mitochondrial and from mitochondrial to unlabelled microsomal membranes was studied using partially purified cytosol proteins isolated from guinea pig liver cytosol. In the absence and presence of these proteins the amounts of phosphatidylinositol transfer from microsomal to mitochondrial membranes were approximately 21 and 33%, respectively, and the amounts from mitochondrial to microsomal membranes were approximately 31 and 39%, respectively. The release of phosphatidyl-[2′-3H]inositol from microsomal membranes in the absence of mitochondria was dependent on concentration of cytosol proteins. Two mechanisms for movement between membranes are proposed. In cytosol-protein-independent movement of phosphatidyl-[2′-3H]inositol from microsomal to mitochondrial membranes, a direct contact between membranes is required, since phosphatidyl-[2′-3H]inositol was not detected in the reaction medium. In the cytosol-protein-catalyzed transfer, formation of phosphatidyl-[2′-3H]inositol – cytosol protein complex is postulated, since phosphatidyl-[2′-3H]inositol was released into the reaction medium and its movement proceeded from mitochondrial to microsomal membranes in the presence of partially purified cytosol proteins. Thus, contact between the two membranes is probably not necessary for this transfer. Implications for the movement of phospholipids between biological membranes are discussed.

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