Variable expression of glutathione S-transferase isoenzymes in the fungus, Mucor circinelloides

Glutathione S-transferase isoenzymes from Streptomyces griseus.

An inducible, cytosolic glutathione S-transferase (GST) was purified from Streptomyces griseus. GST isoenzymes with pI values of 6.8 and 7.9 used standard GST substrates including 1-chloro-2,4-dinitrobenzene. GST had subunit and native M(r)s of 24 and 48, respectively, and the N-terminal sequence SMILXYWDIIRGLPAH.

Glutathione S-transferase isoenzymes in rat brain neurons and glia.

The glutathione S-transferases (GSTs) constitute a family of cytosolic isoenzymes and a structurally unrelated microsomal enzyme that is involved in the detoxication of electrophilic xenobiotics. These enzymes also participate in the intracellular binding and transport of a broad range of lipophilic compounds including bilirubin, and hormones such as the glucocorticoids and thyroid hormones. Th...

Expression of cytochrome P450 and glutathione S-transferase in human bone marrow mesenchymal stem cells

Currently several studies are being carried out on various properties of mesenchymal stem cells (MSCs)however there are a few investigations about drug metabolizing properties of these cells. The aim of thisstudy was to measure the key factors involved in drug metabolism in human bone marrow MSCs. For thispurpose, cellular glutathione (GSH), glutathione Stransferase (GSTs) and...

Mucor circinelloides Growth and Differentiation in the Fungus A Subunit of Protein Kinase A Regulates

Effects of hyperbilirubinaemia on glutathione S-transferase isoenzymes in cerebellar cortex of the Gunn rat.

The glutathione S-transferases (GSTs) are a family of isoenzymes involved in the detoxication of a variety of electrophilic xenobiotics. The present investigation demonstrates that GST activity and the concentration of cytosolic GSTs in cerebellar cortex of Gunn rats were increased in hyperbilirubinaemic animals compared with non-jaundiced controls. Age-dependent and region-specific increases i...