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Related Experiment Videos

Cathepsin G from human polymorphonuclear leukocytes cleaves human IgM.

A Baici, M Knöpfel, K Fehr

    Molecular Immunology
    |May 1, 1982
    PubMed
    Summary

    Cathepsin G, an enzyme from human white blood cells, breaks down human immunoglobulin M (IgM) into fragments similar to those produced by leukocyte elastase. This study details the cleavage products and their characteristics.

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    Area of Science:

    • Immunology
    • Biochemistry
    • Enzymology

    Background:

    • Human polymorphonuclear leukocytes contain cathepsin G, a chymotrypsin-like enzyme.
    • Leukocyte elastase also digests human immunoglobulin M (IgM).

    Purpose of the Study:

    • To investigate the cleavage of human IgM by cathepsin G.
    • To compare the resulting fragments with those produced by leukocyte elastase.

    Main Methods:

    • Enzymatic digestion of human IgM with cathepsin G.
    • Analysis of cleavage fragments using molecular weight determination and immunochemical analysis.

    Main Results:

    • Cathepsin G produced two major fragments: an F(ab)2 mu-like fragment (140,000 mol. wt) and an Fab mu-like fragment (54,000 mol. wt).

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  • These fragments were immunochemically indistinguishable from those generated by leukocyte elastase.
  • Cathepsin G cleaved IgM to produce Fab mu fragments faster than F(ab)2 mu fragments, unlike elastase.
  • A product identical to the IgM subunit was also released.

    • Conclusions:

    • Cathepsin G and leukocyte elastase generate similar IgM fragments.
    • The kinetics of cleavage differ between cathepsin G and elastase.
    • The biological significance of IgM interaction with leukocyte proteinases warrants further discussion.