Literature DB >> 8448991

Species difference in hydroperoxide-scavenging enzymes with special reference to glutathione peroxidase in guinea-pigs.

S Himeno1, A Takekawa, N Imura.   

Abstract

1. As guinea-pigs have been reported to have a markedly low activity of glutathione peroxidase (GSH-Px), the activity of other hydroperoxide-scavenging enzymes was investigated. 2. Catalase activity in guinea-pig tissues was 2-3 times higher than that of mice or rats. 3. Approximately 90% of catalase activity was found in the soluble fraction of guinea-pig liver, suggesting a compensatory role of catalase in removing H2O2 in the cytosol of guinea-pig tissues. 4. In erythrocytes, GSH-Px activity does not differ among rodents. This may reflect the fact that GSH-Px is the sole enzyme in the removal of organic hydroperoxides in erythrocytes where glutathione S-transferase activity is barely detectable.

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Year:  1993        PMID: 8448991     DOI: 10.1016/0305-0491(93)90334-2

Source DB:  PubMed          Journal:  Comp Biochem Physiol B        ISSN: 0305-0491


  2 in total

1.  Inhibition of gamma-glutamyltranspeptidase decreases renal deposition of mercury after mercury vapor exposure.

Authors:  C Y Kim; C Watanabe; Y Kasanuma; H Satoh
Journal:  Arch Toxicol       Date:  1995       Impact factor: 5.153

2.  Fibroblasts from naked mole-rats are resistant to multiple forms of cell injury, but sensitive to peroxide, ultraviolet light, and endoplasmic reticulum stress.

Authors:  Adam B Salmon; Amir A Sadighi Akha; Rochelle Buffenstein; Richard A Miller
Journal:  J Gerontol A Biol Sci Med Sci       Date:  2008-03       Impact factor: 6.053

  2 in total

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