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Angiotensin I-converting enzyme in human placenta.

H Taira, S Mizutani, O Narita

    Placenta
    |November 1, 1985
    PubMed
    Summary

    Human placental angiotensin I-converting enzyme (ACE) was purified and characterized. Affinity chromatography using Captopril enabled extensive purification of this enzyme, revealing its polymeric structure.

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    Area of Science:

    • Biochemistry
    • Enzymology

    Background:

    • Angiotensin I-converting enzyme (ACE) plays a crucial role in the renin-angiotensin system.
    • ACE is also known as peptidyldipeptide hydrolase or kininase II.
    • Understanding ACE structure and function is vital for cardiovascular research.

    Purpose of the Study:

    • To purify and characterize angiotensin I-converting enzyme (ACE) from human placenta.
    • To investigate the effectiveness of Captopril in ACE purification.

    Main Methods:

    • Purification of ACE using affinity chromatography with Captopril.
    • Estimation of molecular weight via high-performance gel permeation chromatography.
    • Determination of subunit size using sodium dodecyl sulphate gel electrophoresis.

    Main Results:

    • ACE was purified 6297-fold from human placenta.
    • Captopril proved to be an effective agent for extensive ACE purification.
    • The enzyme exhibits a polymeric structure with an estimated molecular weight of 300,000 and subunit size of 85,000.

    Conclusions:

    • Human placental ACE can be effectively purified using Captopril-affinity chromatography.
    • The characterized ACE is a polymeric enzyme.
    • This purification and characterization provide insights into ACE structure relevant to its function.

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