In vitro effect of oxidized and reduced glutathione peptides on angiotensin converting enzyme purified from human plasma

Angiotensin converting enzyme (ACE, peptidyldipeptidase A, EC 3.4.15.1) plays an important role in the regulation of blood pressure. In this study, ACE was purified from human plasma by affinity chromatography in single step. The enzyme purified in 5367-fold from human plasma and specific activity was found to be 1208 EU/mg protein. The purity and molecular weight of ACE were determined by SDS-PAGE, which indicated two bands at around 60 kDa and 70 kDa on the gel. Effect of oxidized glutathione (GSSG) peptide and reduced glutathione (GSH) peptide on purified ACE activity were also investigated in which lisinopril was used as reference inhibitor. GSSG showed activation effect on ACE activity whereas GSH provided inhibition effect. In the lights of activity (%) versus activator graph for GSSG and activity (%) versus inhibitor graphs for GSH and lisinopril; IC50 values for GSH and lisinopril were determined to be 16.2 μM and 0.781 nM, respectively. Type of inhibition for GSH and lisinopril from graph Lineweaver-Burk was found to be reversible non-competitive inhibition and Ki constants for GSH and lisinopril were calculated as 11.7 μM and 0.662 nM, respectively. •Angiotensin converting enzyme was 5367-fold purified by affinity chromatography from human plasma.•The purity and molecular weight of ACE was determined by SDS-PAGE.•GSSG showed activation effect on ACE activity while GSH showed inhibition effect.•IC50 and Ki values for GSH peptide was calculated to de 16.2 μM and 11.7 μM, respectively.