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Radiolabelled substrates for angiotensin converting enzyme.

A Y Chung, J W Ryan, J P Ryan

    Advances in Experimental Medicine and Biology
    |January 1, 1986
    PubMed
    Summary

    Researchers developed new [3H]benzoyl-tripeptides as substrates for angiotensin converting enzyme (ACE). These substrates allow for direct measurement of enzyme kinetics in vitro and in vivo, aiding ACE research.

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    Area of Science:

    • Biochemistry
    • Enzymology
    • Pharmacology

    Background:

    • Angiotensin converting enzyme (ACE) plays a crucial role in the renin-angiotensin system.
    • Developing reliable substrates is essential for studying ACE kinetics and inhibition.
    • Previous ACE substrates had limitations in kinetic analysis.

    Purpose of the Study:

    • To synthesize and characterize novel [3H]benzoyl-tripeptide substrates for ACE.
    • To evaluate the utility of these substrates for measuring ACE kinetics under first-order conditions.
    • To compare in vitro kinetic parameters with in vivo substrate utilization rates.

    Main Methods:

    • Synthesis of six [3H]benzoyl-tripeptides via catalytic dehalogenation of iodo-analogs.
    • Kinetic parameter measurements using purified human and rabbit ACE at 37°C.
    • Assay buffer: 0.05 M Hepes, pH 8.0, 0.1 M NaCl, 0.6 M Na2SO4.
    • In vivo studies using anesthetized rats to assess substrate utilization in lung passage.

    Main Results:

    • The synthesized [3H]benzoyl-tripeptides functioned effectively as ACE substrates.
    • Relative kinetic values (Kc/Km) were consistent between human and rabbit ACE.
    • In vivo substrate utilization rates in rats mirrored the in vitro relative kinetic values.
    • First-order enzyme kinetics were achievable with these substrates.

    Conclusions:

    • A new series of ACE substrates has been developed for both in vitro and in vivo applications.
    • These substrates enable direct measurement of V/Km and Ki under first-order kinetics.
    • The findings facilitate more accurate and direct kinetic analysis of ACE activity.

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