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Kinin cleavage by human erythrocytes.

W Sidorowicz, P C Canizaro, F J Bĕhal

    American Journal of Hematology
    |January 1, 1984
    PubMed
    Summary

    Human red blood cells contain aminopeptidase-P, an enzyme that cleaves arginine from bradykinin. This enzyme is stable and abundant within erythrocytes, suggesting a significant role in blood kinin metabolism.

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    Area of Science:

    • Biochemistry
    • Enzymology
    • Human Physiology

    Background:

    • Aminopeptidase-P plays a role in peptide metabolism.
    • Bradykinin is a vasoactive peptide involved in blood pressure regulation.
    • Erythrocytes are known to possess various enzymatic activities.

    Purpose of the Study:

    • To purify and characterize aminopeptidase-P from human erythrocytes.
    • To investigate the presence and activity of aminopeptidase-P in intact erythrocytes.
    • To compare the erythrocyte enzyme's activity to other tissues.

    Main Methods:

    • Purification of aminopeptidase-P from human erythrocytes using standard biochemical techniques.
    • Enzyme characterization including molecular weight determination, pH optimum, and cofactor requirements.
    • Assay of enzyme activity using des-(Arg9)-bradykinin and various X-proline dipeptides.
    • Quantification of total intra-erythrocytic enzyme activity.

    Main Results:

    • Aminopeptidase-P was purified 230-fold from human erythrocytes.
    • The enzyme exhibited a molecular weight of 155,000 +/- 6,900 daltons, pH optimum of 7.2, and was stimulated by manganous ions.
    • Intact erythrocytes cleaved arginine from des-(Arg9)-bradykinin, with arginine as the earliest product.
    • Erythrocytes contain significant aminopeptidase-P activity, exceeding that of the total lung mass.
    • The enzyme was stable in erythrocytes for at least 21 days and not tightly bound to the membrane.

    Conclusions:

    • Human erythrocytes possess a stable and active form of aminopeptidase-P.
    • Erythrocyte aminopeptidase-P contributes significantly to kinin metabolism.
    • The enzyme's abundance suggests a potentially crucial physiological role in the blood.

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