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. 1984 Sep 1;222(2):553–556. doi: 10.1042/bj2220553

Studies on the glutathione S-transferase activity associated with rat liver mitochondria.

C M Ryle, T J Mantle
PMCID: PMC1144210  PMID: 6477531

Abstract

The major proportion of rat liver glutathione S-transferase is cytosolic. Carefully washed mitochondria contain 0.25-0.47% of the cytosolic activity. Subfractionation of washed mitochondria using digitonin treatment revealed that glutathione S-transferase release did not parallel that of any of the mitochondrial marker enzymes. Glutathione S-transferase release paralleled that of lactate dehydrogenase, suggesting that these 'mitochondrial' activities are due to loosely bound cytoplasmic forms.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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