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  • Title: Angiotensin I-converting enzyme in human placenta.
    Author: Taira H, Mizutani S, Narita O, Tomoda Y.
    Journal: Placenta; 1985; 6(6):543-9. PubMed ID: 3014488.
    Abstract:
    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.
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