ISSN:
1432-0738
Keywords:
Key words Glutathione S-transferase
;
Erythrocytes
;
Human
Source:
Springer Online Journal Archives 1860-2000
Topics:
Medicine
Notes:
Abstract A new polymorphic form of glutathione S-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 θ 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 θ 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 and p-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 common N-terminal modification which modifies substrate binding. The new polymorphic GST-isoform in human red blood cells therefore may be considered to represent an N-terminally modified isoform of GST T1-1.
Type of Medium:
Electronic Resource
