Abstract
Peroxyacetyl nitrate reacts with reduced glutathione producing oxidized glutathione and S-acetyl glutathione. Reaction of peroxyacetyl nitrate with reduced coenzyme A results in the formation of coenzyme A disulfide, accounting for 35–45% of the reacted sulfhydryl. The remaining products can be separated by ion exchange chromatography and are probably higher oxidation states. There is no evidence of formation of S-acetyl coenzyme A. The distribution of products obtained by treatment of coenzyme A with peroxyacetyl nitrate is similar to that obtained by treatment of coenzyme A with hydrogen peroxide. Treatment of proteins with peroxyacetyl nitrate has not provided any evidence of acetylation of sulfhydryl groups detectable by the hydroxamate test. Intramolecular disulfide bonds are formed by treatment of reduced ribonuclease with peroxyacetyl nitrate but no evidence has been obtained in favor of formation of intermolecular disulfide bonds.
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