Angiotensin I-converting enzyme in human placenta.
Angiotensin I-converting enzyme (ACE, peptidyldipeptide hydrolase, kininase II, EC 3.4.15.I) from human placenta was purified 6297-fold and characterized. ACE could be extensively purified by affinity chromatography with Captopril (D-3-mercapto-2-methylpropanoyl-L-proline), an orally active antihypertensive agent and a potent inhibitor of this enzyme. Its molecular weight and subunit size were estimated to be 300 000 by high-performance gel permeation chromatography and 85 000 by sodium dodecyl sulphate gel electrophoresis, respectively, indicating its polymeric structure.
D002216:Captopril; D002846:Chromatography, Affinity; D005260:Female; D006801:Humans; D008970:Molecular Weight; D007703:Peptidyl-Dipeptidase A / Q000302:isolation & purification*; D010920:Placenta / Q000201:enzymology*; D011247:Pregnancy; D011487:Protein Conformation
D002216:Captopril; D007703:Peptidyl-Dipeptidase A