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Related Experiment Videos

A novel proteolytic activity in serum processes rat prohaptoglobin.

J M Hanley, E C Heath

    Archives of Biochemistry and Biophysics
    |June 1, 1985
    PubMed
    Summary

    Rat haptoglobin (prohaptoglobin) is processed into its active form by a novel plasma proteolytic activity. This protease, likely secreted by hepatocytes, functions similarly to the intracellular enzyme.

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    Area of Science:

    • Biochemistry
    • Proteomics
    • Molecular Biology

    Background:

    • Rat haptoglobin is a plasma glycoprotein synthesized as a precursor, prohaptoglobin, by hepatocytes.
    • Prohaptoglobin undergoes intracellular processing to yield the mature tetrameric protein.

    Purpose of the Study:

    • To investigate a novel proteolytic activity found in rat plasma and serum.
    • To characterize the properties and potential origin of this plasma protease.

    Main Methods:

    • Analysis of proteolytic activity in rat plasma and serum.
    • Site-specific cleavage assays on prohaptoglobin.
    • Characterization of protease inhibition by sulfhydryl-reactive compounds.

    Main Results:

    • A novel proteolytic activity in rat plasma/serum cleaves prohaptoglobin at the same site as the intracellular protease.
    • This activity is not a serine protease or metalloenzyme, but is inhibited by sulfhydryl-reactive compounds.
    • The protease is synthesized and secreted by hepatocytes, suggesting identity with the intracellular processing enzyme.

    Conclusions:

    • Rat plasma contains a specific protease capable of processing prohaptoglobin.
    • This protease is likely hepatocyte-derived and may be the same enzyme responsible for intracellular prohaptoglobin maturation.

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