Glutathione-dependent fatty acylprotein deacylase

Abstract

Monkey intestinal brush border membrane (BBM) when incubated with reduced glutathione (GSH), was found to release covalently bound fatty acids. However this activity was greatly reduced with delipidated BBM and nonexistent with heat-treated BBM. This release was specific for GSH since other thiol compounds such as DTT, cysteine, or oxidized glutathione could not do so. There was a concentration-dependent increase in deacylation with increasing concentration of GSH. Deacylation was pH dependent, and maximum activity was seen at pH 7.5. These results indicate that possibly a glutathione-dependent enzyme is involved in deacylation of membrane proteins and this may have a role in the turnover of fatty acid-acylated proteins.