THROMBOSTHENIN-A CONTRACTILE PROTEIN FROM THROMBOCYTES - ITS EXTRACTION FROM HUMAN BLOOD PLATELETS AND SOME OF ITS PROPERTIES
THROMBOSTHENIN-A CONTRACTILE PROTEIN FROM THROMBOCYTES - ITS EXTRACTION FROM HUMAN BLOOD PLATELETS AND SOME OF ITS PROPERTIES
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DOI:
10.1016/0006-3002(61)90250-5
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发表时间:
1961-01-01
期刊:
影响因子:
--
通讯作者:
LUSCHER, EF
中科院分区:
文献类型:
--
作者:
BETTEXGALLAND, M;LUSCHER, EF
On extraction of human blood platelets with a buffered 0.6[image] KC1 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 contracile 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 Ca2+ and Mg2+ 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.