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Plasminogen: purification from human plasma by affinity chromatography.

D G Deutsch, E T Mertz

    Science (New York, N.Y.)
    |December 4, 1970
    PubMed
    Summary
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    Researchers purified plasminogen from human plasma using affinity chromatography. This method yielded highly purified plasminogen with significant caseinolytic activity, demonstrating its effectiveness for protein preparation.

    Area of Science:

    • Biochemistry
    • Protein Chemistry
    • Chromatography

    Background:

    • Plasminogen is a crucial precursor protein in the fibrinolytic system.
    • Efficient purification of active plasminogen is essential for research and therapeutic applications.

    Purpose of the Study:

    • To develop and validate a method for purifying active plasminogen from human plasma.
    • To characterize the purity and activity of the prepared plasminogen.

    Main Methods:

    • Affinity chromatography utilizing L-lysine-substituted Sepharose was employed for plasminogen isolation.
    • Caseinolytic activity assays were performed to quantify enzyme function.
    • Disc-gel electrophoresis was used to assess protein purity and identify active components.

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    Main Results:

    • Thirty milligrams of plasminogen were successfully purified from 340 milliliters of human plasma.
    • The purified plasminogen exhibited a specific activity of 100 caseinolytic units per milligram of nitrogen.
    • Over 200-fold purification was achieved, with disc-gel electrophoresis revealing seven active bands.

    Conclusions:

    • Affinity chromatography on L-lysine-Sepharose is a highly effective method for purifying active human plasminogen.
    • The developed protocol yields a significantly purified and enzymatically active plasminogen preparation.
    • This purified plasminogen is suitable for further biochemical and potentially clinical investigations.