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Related Experiment Videos

Nonplasminogen-dependent protease in human plasma.

J A Marcum, D L Kline

    Blood
    |September 1, 1979
    PubMed
    Summary
    This summary is machine-generated.

    A novel caseinolytic protease was generated from plasma euglobulin precipitates. This protease, distinct from plasmin or coagulation factors, exhibits specific inhibition patterns and a pH optimum of 6.5.

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    Area of Science:

    • Biochemistry
    • Protease research
    • Plasma protein analysis

    Background:

    • Plasma contains numerous enzymes and zymogens.
    • The generation of proteolytic activity from plasma components is complex.
    • Characterization of novel proteases is crucial for understanding biological processes.

    Purpose of the Study:

    • To investigate the generation and properties of a novel caseinolytic protease from plasma.
    • To differentiate this protease from known plasma enzymes like plasmin and coagulation factors.
    • To determine the optimal conditions and inhibitors for the generated protease.

    Main Methods:

    • Plasma euglobulin fractions were incubated with potassium phosphate buffer and adjusted to specific pH.
    • Caseinolytic activity was measured using a standard assay.

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  • Inhibition studies were performed using diisopropylphosphofluoridate, pancreatic trypsin inhibitor, and soybean trypsin inhibitor.
  • Protease generation was assessed in plasmas deficient in specific coagulation factors and plasminogen.

    • Main Results:

    • A caseinolytic protease with activity of 0.05 CTA U/ml was generated from plasma euglobulin precipitate.
    • The protease exhibited a pH optimum of 6.5, with activity declining below pH 6.0 and above 7.4.
    • Activity was inhibited by diisopropylphosphofluoridate and pancreatic trypsin inhibitor, but not by soybean trypsin inhibitor.
    • The protease was generated independently of plasminogen, Hageman factor (factor XII), factor XI, factor VII, prekallikrein, thrombin, and purified Cl-esterase.
    • The generated protease showed no procoagulant or fibrinolytic activity.

    Conclusions:

    • A novel, salt-dependent caseinolytic protease can be generated from plasma euglobulin precipitates.
    • This protease is distinct from plasmin and other known coagulation or contact activation factors.
    • The specific inhibition profile suggests a serine protease distinct from trypsin.
    • The findings indicate a previously uncharacterized proteolytic pathway in plasma.