| Autor: |
Schröder, Klaus R., Hallier, Ernst, Meyer, David J., Wiebel, Frederike A., Müller, Andreas M. F., Bolt, Hermann M. |
| Zdroj: |
Archives of Toxicology; July 1996, Vol. 70 Issue: 9 p559-566, 8p |
| Abstrakt: |
A new polymorphic form of glutathioneS-transferase (GST), metabolising monohalogenated methanes, ethylene oxide and dichloromethane, has been purified from human erythrocytes and characterized. Several characteristics, such as similar elution patterns on different chromatographic matrices, KM-values and activity towards antibodies, confirm a previous assumption that this novel GST is a class δ enzyme. Although the presence or absence of the enzyme activity in human red blood cells is parallel with the polymorphism of the human GST T1 gene, the new GST δ in red blood cells may differ from the known GST T1-1 enzyme from other tissues in terms of substrate specificity, since established GST T1-1 substrates [1,2-epoxy-3-(p-nitro-phenoxy)propane andp-nitrobenzyl chloride] are not metabolized. The substrate specifity of the new enzyme in erythrocytes resembles more closely that of GST T2-2, most likely due to a commonN-terminal modification which modifies substrate binding. The new polymorphic GST-isoform in human red blood cells therefore may be considered to represent anN-terminally modified isoform of GST T1-1. |
| Databáze: |
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