Abstract
On extraction of human blood platelets with a buffered 0.6 M KCl solution, a protein fraction is obtained, which becomes insoluble at ionic strengths below 0.2. If ATP is present, this material will show the phenomenon of superprecipitation or active contraction. Because of its role in thrombocyte function, we have named this contractile protein thrombosthenin. Like actomyosin from muscle, thrombosthenin acts as an ATP-ase. The dependence of this enzymic activity on the ionic strength, on the concentrations of Ca 2+ and Mg 2+ ions, and of ATP has been investigated. The sensitivity of solutions of thrombosthenin towards ATP has been determined. Although the obtained results suggest that thrombosthenin belongs to the actomyosin group, a quantitative comparison with the data on muscle actomyosin leads to the conclusion,, that thrombosthenin is distinct from the contractile protein of muscle. The significance of the presence of thrombosthenin in blood platelets in relation to viscous metamorphosis and clot retraction is discussed.
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