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Carbonic anhydrase in human platelets.

W Siffert, G Gros

    The Biochemical Journal
    |February 1, 1984
    PubMed
    Summary
    This summary is machine-generated.

    Human platelets contain carbonic anhydrase II, which significantly accelerates carbon dioxide (CO2) hydration by 2500-fold. This enzyme is crucial for platelet function and CO2 transport.

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    Area of Science:

    • Biochemistry
    • Physiology

    Background:

    • Carbonic anhydrase (CA) is a metalloenzyme catalyzing CO2 hydration.
    • Platelets play roles in hemostasis, thrombosis, and inflammation.
    • The presence and activity of CA in human platelets were not well-characterized.

    Purpose of the Study:

    • To investigate the carbonic anhydrase activity in human platelets.
    • To determine the kinetic properties and identify the specific CA isoenzyme present in platelets.

    Main Methods:

    • Measurement of CO2 hydration kinetics in platelet lysates using a pH stopped-flow apparatus.
    • Determination of enzyme concentration, Michaelis constant (Km), catalytic-centre activity (kcat), and inhibition constant (Ki).
    • Affinity chromatography to identify the specific carbonic anhydrase isoenzyme.

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    Main Results:

    • An average carbonic anhydrase concentration of 2.1 microM was found in human platelets.
    • Kinetic analysis revealed a Km of 1.0 mM, kcat of 130,000 s-1, and Ki towards ethoxzolamide of 0.3 nM.
    • Affinity chromatography identified carbonic anhydrase II as the predominant isoenzyme, with carbonic anhydrase I being absent.

    Conclusions:

    • Human platelets possess significant carbonic anhydrase activity, primarily due to carbonic anhydrase II.
    • This enzymatic activity accelerates CO2 hydration within platelets by an estimated 2500-fold.
    • The findings suggest a critical role for platelet carbonic anhydrase in physiological processes involving CO2 transport and pH regulation.