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Aminopeptidases from human leucocytes.

W Rautenberg, H Tschesche

    Hoppe-Seyler'S Zeitschrift Fur Physiologische Chemie
    |January 1, 1984
    PubMed
    Summary
    This summary is machine-generated.

    Researchers isolated six aminopeptidases from human leucocyte cytosol, characterizing their specificities and molecular masses. This work provides insights into leucocyte enzyme functions and potential roles in biological processes.

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    Area of Science:

    • Biochemistry
    • Enzymology
    • Human Physiology

    Background:

    • Aminopeptidases are crucial enzymes involved in protein metabolism.
    • Leucocytes play a vital role in the immune system.
    • Understanding leucocyte enzymes can reveal insights into cellular functions and disease.

    Purpose of the Study:

    • To detect and isolate aminopeptidases from human leucocyte cytosol.
    • To characterize the enzymic specificity and physical properties of these isolated enzymes.
    • To differentiate between cytosolic and membrane-bound leucocyte aminopeptidases.

    Main Methods:

    • Isolation of aminopeptidases from human leucocyte cytosol.
    • Chromatographic separation using DEAE-Sephacel.
    • Purification via gel filtration on Sephacryl S-300.

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  • Enzymic specificity assays using L-amino acid-4-nitroanilides.
  • Determination of molecular masses and inhibition profiles.

    • Main Results:

    • Six distinct aminopeptidases were identified and isolated.
    • Aminopeptidases 1, 2, 4, and 5 were characterized from the cytosol, with distinct specificities and molecular masses (150, 70, 220/70, and 90 kDa, respectively).
    • Aminopeptidase 3, a minor component, was identified as a metalloproteinase from the leucocyte plasma membrane (250 kDa).

    Conclusions:

    • Human leucocyte cytosol contains multiple aminopeptidases with diverse substrate specificities.
    • Distinct cytosolic and membrane-bound aminopeptidases exist within leucocytes.
    • These findings contribute to the understanding of leucocyte enzymatic machinery and function.