Journal of Pharmacobio-Dynamics
Online ISSN : 1881-1353
Print ISSN : 0386-846X
ISSN-L : 0386-846X
DECOMPOSITION OF HYDROPEROXIDES DERIVED FROM MICROSOMES OR LIPOPROTEIN BY GLUTATHIONE PEROXIDASE AND GLUTATHIONE S-TRANSFERASE
TOSHINOBU MIWATETSUO ADACHIKAZUYUKI HIRANOMAMORU SUGIURA
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キーワード: lipoprotein
ジャーナル フリー

1983 年 6 巻 7 号 p. 459-465

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抄録
Protective effects of glutathione peroxidase, glutathione S-transferase purified from human liver and superoxide dismutase against lipid peroxidation were investigated. In the presence of glutathione, lipid hydroperoxides found in microsomal membrane were decomposed by glutathione peroxidase and cationic glutathione S-transferase, but anionic glutathione S-transferase had no effect on them. Superoxide dismutase exhibited antioxidation effect by preventing accumulation of lipid hydroperoxides. Serum lipid hydroperoxides existing in low density lipoprotein fraction were also decomposed by glutathione peroxidase and cationic glutathione S-transferase. These findings suggest that the hydroperoxide level, which has high toxicity, could be controlled by these glutathione-dependent glutathione peroxidase and cationic glutathione S-transferase.
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© The Pharmaceutical Society of Japan
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