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Related Experiment Videos

Plasmin cleaves human beta-casein.

R Greenberg, M L Groves

    Biochemical and Biophysical Research Communications
    |December 14, 1984
    PubMed
    Summary
    This summary is machine-generated.

    Plasmin in human milk cleaves beta-casein into specific fragments, similar to bovine casein. This indicates active endogenous plasmin in milk, impacting casein analysis.

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    Area of Science:

    • Biochemistry
    • Proteomics
    • Human milk composition

    Background:

    • Human beta-casein is a major milk protein.
    • Plasmin is a protease known to cleave proteins.
    • Bovine beta-casein is known to be cleaved by plasmin into gamma-caseins.

    Purpose of the Study:

    • To investigate the cleavage of human beta-casein by plasmin.
    • To determine if endogenous plasmin is active in human milk.
    • To assess the implications of plasmin activity on human milk casein analysis.

    Main Methods:

    • In vitro cleavage of isolated human beta-casein by purified plasmin.
    • Identification of resulting protein fragments using biochemical techniques.
    • Analysis of whole human milk for evidence of plasmin activity.

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    Main Results:

    • Plasmin specifically cleaves human beta-casein into distinct fragments.
    • The cleavage pattern resembles that of bovine beta-casein.
    • A previously isolated human milk protein was identified as a plasmin-cleaved beta-casein fragment.
    • Evidence suggests endogenous plasmin is active in whole human milk.

    Conclusions:

    • Endogenous plasmin actively cleaves human beta-casein in milk.
    • Protease activity must be considered during human casein quantitation.
    • Plasmin activity impacts the isolation of components from human milk.