Peptidyl-Dipeptidase A

DescriptionACE possesses dual actions to convert Ang I to Ang II, and degrade bradykinin. The development of an ACE inhibitor was the first effective drug for hypertension caused by high renin activity. ACE2 was identified as the receptor for the SARS (severe acute respiratory syndrome) coronavirus, which caused an epidemic in 2002–2003. ACE was discovered in the mid-1950s through the observation that the dialysis of plasma and kidney extract with water and saline before incubation produced two separate pressor substances, Ang I and Ang II, respectively. It was discovered for a second time in 1966 during the characterization of a bradykinin (BK)-degrading enzyme from the kidney. This was named kininase II, which later was found to be the same enzyme as ACE. ACE2 was discovered in 2000 when two independent research groups cloned homologous ACE that could convert Ang I to Ang1–9 and yet also be captopril-insensitive.

UsesAngiotensin converting enzyme from rabbit lung has been used:for measuring inhibitory effect of egg white protein hydrolysates on ACE activity by high performance liquid chromatography (HPLC)to measure the ACE inhibition by litchi pericarp and cooked chicken breast using hippuryl-L-histidyl-L-leucine (HHL) as substrate by reverse phase-HPLC (RP-HPLC)3 and HPLC respectively in releasing GPI anchored protein in vitro in few cell lines like HeLa, HEK293 and in vivo in mice sperm.

General DescriptionThe angiotensin-converting enzyme (ACE) is a dipeptidyl-carboxypeptidase which exists in somatic and testicular isoforms with zinc binding motif HEXXH in their active site. ACE regulates blood pressure through renin-angiotensin system. ACE elevates blood pressure by converting angiotensin I to a key vasoconstrictor angiotensin II and inhibiting a potent vasodilator bradykinin. Inhibition of ACE is a targeted therapeutic strategy for high blood pressure. Several ACE synthetic inhibitory peptides available for clinical use include captopril, enalapril and lisinopril. Currently, developing inhibitory peptides from natural food sources, or phenolic compounds from plant sources to inhibit ACE is underway. ACE plays a critical role in fertilization by releasing the proteins anchored to glycosylphosphatidylinositol (GPI) in sperm membrane.

DescriptionACE Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 1235 amino acids (30-1256 a.a.) and having a molecular mass of 142kDa. ACE is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.