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Papain inhibition by serum

M J Fisher, R E Jay, L D Haugh

    Journal of Applied Physiology
    |August 1, 1976
    PubMed
    Summary
    This summary is machine-generated.

    Animal sera inhibit papain activity, with rat serum showing the highest papain inhibitory capacity (PIC). This competitive inhibitor is heat-labile and separable from antitrypsin activity.

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    Area of Science:

    • Biochemistry
    • Enzymology
    • Comparative Immunology

    Background:

    • Papain is a cysteine protease with broad substrate specificity.
    • Serum contains various proteins, including protease inhibitors.
    • Understanding serum's interaction with proteases is crucial for biological and medical research.

    Purpose of the Study:

    • To investigate the presence and characteristics of papain inhibitors in sera from different animal species.
    • To quantify the papain inhibitory capacity (PIC) across species.
    • To determine the nature of the inhibitor (e.g., competitive, heat sensitivity).

    Main Methods:

    • Assaying papain activity using alpha-N-benzoyl-L-arginine-p-nitroaniline hydrochloride (L-BAPA) as a substrate.
    • Measuring inhibition of L-BAPA hydrolysis by sera from rat, cow, cat, dog, human, rabbit, and hamster.

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  • Defining and calculating Papain Inhibitory Capacity (PIC) per ml of serum.
  • Assessing inhibitor properties including heat lability, dialyzability, and competitive kinetics.
  • Separating antipapain activity from antitrypsin activity using ammonium sulfate fractionation.

    • Main Results:

    • All tested animal sera exhibited papain inhibitory activity against L-BAPA hydrolysis.
    • Rat serum demonstrated the highest PIC, while hamster serum showed the lowest.
    • The serum inhibitor acts competitively with respect to the substrate L-BAPA.
    • The inhibitor was found to be heat-labile and nondialyzable.
    • Antipapain activity was successfully separated from antitrypsin activity via ammonium sulfate fractionation.

    Conclusions:

    • Mammalian and non-mammalian sera contain heat-labile, nondialyzable inhibitors of papain.
    • Significant species-dependent variation exists in the concentration of these papain inhibitors.
    • The inhibitor's competitive nature and heat lability provide insights into its biochemical properties.
    • Effective separation of antipapain from antitrypsin activity is achievable, suggesting distinct molecular entities.