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Immunoreactive anionic trypsin and anionic elastase in human milk.

S Borulf, T Lindberg, M Månsson

    Acta Paediatrica Scandinavica
    |January 1, 1987
    PubMed
    Summary
    This summary is machine-generated.

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    Human milk contains anionic trypsin and elastase, detected via immunodiffusion. These enzymes, likely complexed with IgA, showed activity after purification, indicating their presence in breast milk.

    Area of Science:

    • Biochemistry
    • Immunology
    • Human milk analysis

    Background:

    • Human milk contains various enzymes crucial for infant nutrition and protection.
    • Proteases like trypsin and elastase play roles in protein digestion and immune modulation.

    Purpose of the Study:

    • To investigate the presence and characteristics of trypsin and elastase in human milk.
    • To determine the enzymatic activity of these proteases in skim milk and purified fractions.

    Main Methods:

    • Immunodiffusion and immunoelectrophoresis were used to detect immunoreactive anionic and cationic trypsin and elastase.
    • Immunoadsorption chromatography was employed for the isolation of anionic trypsin.
    • Benzoyl-DL-arginine-p-nitroanilide (BAPNA) was used to assess enzyme activity.

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    Main Results:

    • Immunoreactive anionic trypsin and anionic elastase were detected in human milk.
    • Cationic forms of trypsin and elastase were not detected by the applied immunological methods.
    • Anionic trypsin was isolated and demonstrated benzoyl-DL-arginine-p-nitroanilide (BAPNA)-splitting activity, suggesting functional relevance.
    • No BAPNA-splitting activity was observed in human skim milk prior to enzyme isolation.

    Conclusions:

    • Human milk contains immunoreactive anionic trypsin and elastase, likely associated with IgA.
    • The functional BAPNA-splitting activity of anionic trypsin is confirmed upon purification.
    • Further research is warranted to elucidate the specific roles of these milk proteases in infant health.