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Affinity purification of kallikrein and elastase from hog pancrease powder.

T Honda, A Fujita, Y Tsubakihara

    Journal of Chromatography
    |April 11, 1986
    PubMed
    Summary
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    This study presents an efficient method for isolating hog pancreas kallikrein and elastase. The developed technique achieved significant activity yields for both crucial enzymes.

    Area of Science:

    • Biochemistry
    • Enzymology

    Background:

    • Kallikrein and elastase are vital proteases with diverse physiological roles.
    • Efficient isolation methods are crucial for biochemical research and therapeutic applications.

    Purpose of the Study:

    • To develop an efficient method for the simultaneous isolation of kallikrein and elastase from hog pancreas.
    • To characterize the isolated enzymes.

    Main Methods:

    • Simultaneous enzyme isolation using successive column chromatography (CM-cellulofine, p-aminobenzamidine-Sepharose 4B).
    • Further purification of kallikrein via DEAE-Sephadex chromatography.
    • Elastase purification through repeated Sephadex G-75 gel chromatography.
    • Analysis of enzyme purity using SDS-PAGE.

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    Main Results:

    • Successful simultaneous isolation of kallikrein and elastase.
    • Kallikrein resolved into two components by SDS-PAGE; elastase showed a single component.
    • Achieved activity yields of 49% for kallikrein and 38% for elastase.

    Conclusions:

    • The described method is effective for simultaneous kallikrein and elastase isolation from hog pancreas.
    • The purification strategy yields enzymes of distinct purity profiles.
    • This method provides a valuable tool for obtaining these enzymes for further study.