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Related Experiment Videos

Human lysosomal elastase. Catalytic and immunological properties

P M Starkey, A J Barrett

    The Biochemical Journal
    |May 1, 1976
    PubMed
    Summary

    Human spleen elastase functions as a serine proteinase, similar to porcine pancreatic elastase. This enzyme is immunologically identical to lysosomal elastase found in human neutrophil leucocytes.

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    Area of Science:

    • Biochemistry
    • Enzymology

    Background:

    • Elastase enzymes play crucial roles in various physiological processes.
    • Understanding the characteristics of human spleen elastase is important for its potential applications.

    Purpose of the Study:

    • To characterize the enzymatic activity and properties of human spleen elastase.
    • To compare human spleen elastase with other known elastases.

    Main Methods:

    • Assessing endopeptidase activity against azo-casein and elastin.
    • Evaluating activity using synthetic substrates like benzyloxycarbonyl-L-alanine 2-naphthyl ester.
    • Determining the optimal pH range for enzyme activity.
    • Investigating inhibitor effects to classify the enzyme.
    • Raising specific antisera for immunological comparison.

    Main Results:

    • Human spleen elastase exhibits endopeptidase activity on azo-casein and elastin.
    • Benzyloxycarbonyl-L-alanine 2-naphthyl ester is identified as a suitable substrate.
    • The enzyme has a broad pH optimum between 8.2-9.2.
    • Inhibitor studies reveal it to be a serine proteinase with specificity akin to porcine pancreatic elastase.
    • Immunological studies confirm identity with human neutrophil leucocyte lysosomal elastase.

    Conclusions:

    • Human spleen elastase is a serine proteinase with characteristics similar to porcine pancreatic elastase.
    • It is immunologically indistinguishable from lysosomal elastase in human neutrophils.

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