Nitroglycerin (GTN) has been used as the drug of choice in the treatment of angina pectoris. It has been shown that some glutathione S-transferases (GSTs) catalyze the metabolic conversion from GTN to glyceryl dinitrates (GDNs). In this study, we examined the substrate specificity of GSTs for GTN. Alpha and mu GSTs were isolated from porcine liver and intestinal mucosa by means of CM-cellulose and glutathione-affinity column chromatography. Mu GSTs degraded GTN time-dependently and formed 1,3-GDN in preference to 1,2-GDN as a ratio (1,2-GDN/ 1,3-GDN) of 0.61, whereas alpha GSTs formed twice as much 1,2-GDN as 1,3-GDN. These results showed that two GST families participate in the metabolic conversion of GTN at different hydrolyzing portions of the nitrogroups.
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