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. 1970 Sep;119(3):463–472. doi: 10.1042/bj1190463

Enzyme-catalysed reactions between some 2-substituted 5-nitrofuran derivatives and glutathione

E Boyland 1, B E Speyer 1
PMCID: PMC1179375  PMID: 5533198

Abstract

1. A glutathione transferase present in rat and human liver supernatant catalyses the reaction of some 2-substituted 5-nitrofuran derivatives with GSH, with formation of a conjugate and release of the nitro group as inorganic nitrite. Some of the substrates undergo the same reaction at a slower rate in the absence of enzyme. Nitrofuran derivatives commonly used as drugs, and five other drugs containing nitro groups, did not react. 2. Substrate activity in the nitrofuran derivatives showed an approximate correlation with the lability of the nitro group to alkali. 3. Optimum pH values ranging from 6.6 to 9.0 were found for the enzymic reaction with various derivatives, the values being influenced by alkali-lability and pK values of the compounds. 4. Tenfold purification of rat liver glutathione S-aryl-transferase resulted in an equal purification of the activities that catalyse the reaction of two of the nitrofuran derivatives with GSH.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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