Isoenzyme profile of glutathione S-transferases in human kidney
β Scribed by Simic, Tatjana ;Mimic-Oka, Jasmina ;Ille, Katarina ;Savic-Radojevic, Ana ;Reljic, Zorica
- Publisher
- Springer
- Year
- 2001
- Tongue
- English
- Weight
- 129 KB
- Volume
- 29
- Category
- Article
- ISSN
- 0300-5623
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π SIMILAR VOLUMES
Qualitative and quantitative changes in glutathione S-transferase (GSH-T) were studied in human hepatocellular carcinoma. GSH-T specific activity (mumoles per min per mg protein) was variably reduced in hepatocellular carcinoma. Similar changes were seen in "cationic" GSH-T (ligandin) concentration
Trivalent antimony (SB β«3β¬ ) in the form of potassium antimony tartrate was found to be an inhibitor of glutathione-S-transferases (GST) from human erythrocytes with a 50% inhibition concentration (IC 50 ) of 0.05 mM. The inhibition was, however, incomplete with 15-20% of the GST activity remaining