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Related Experiment Videos

Human liver cathepsin L.

R W Mason, G D Green, A J Barrett

    The Biochemical Journal
    |February 15, 1985
    PubMed
    Summary
    This summary is machine-generated.

    Researchers purified human cathepsin L, a key enzyme, from liver tissue. This purification and characterization will aid in identifying cathepsin L in various tissues and species.

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    Leukemia & lymphoma·2016

    Area of Science:

    • Biochemistry
    • Enzymology

    Background:

    • Cathepsin L is a cysteine protease implicated in various biological processes.
    • Understanding its structure and function is crucial for biological research.

    Purpose of the Study:

    • To purify and characterize human cathepsin L.
    • To establish key properties for enzyme identification.

    Main Methods:

    • Purification of human liver homogenate.
    • Ion-exchange chromatography (Carboxymethyl-Sephadex, Mono S).
    • Analysis of enzyme kinetics and inactivation.

    Main Results:

    • Human cathepsin L was purified to homogeneity.
    • The enzyme consists of two polypeptide chains (25 kDa and 5 kDa).
  • Kinetic properties are similar to rat and rabbit cathepsin L.

    • Conclusions:

    • Detailed characteristics of human cathepsin L have been established.
    • These findings facilitate the identification of cathepsin L in other biological contexts.