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  • 1
    Digitale Medien
    Digitale Medien
    [s.l.] : Nature Publishing Group
    Nature 298 (1982), S. 202-202 
    ISSN: 1476-4687
    Quelle: Nature Archives 1869 - 2009
    Thema: Biologie , Chemie und Pharmazie , Medizin , Allgemeine Naturwissenschaft , Physik
    Notizen: [Auszug] IN a recent letter1 it was shown that cytochalasin D inhibits and reverses the formation of thrombin-induced actin filaments in platelets. It was noted also that SDS-polyacrylamide gels of reduced samples of Triton-insoluble residue from thrombin-treated platelets showed additional protein bands ...
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 3 (1983), S. 21-30 
    ISSN: 0886-1544
    Schlagwort(e): platelets ; Triton-insoluble residue ; fibrinogen ; fibrin ; tubulin ; cytoskeleton ; Life and Medical Sciences ; Cell & Developmental Biology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie , Medizin
    Notizen: Several proteins (eg, actin, myosin, and actin-binding protein) in the Tritoninsoluble residue of thrombin-stimulated platelets are important in the formation of cytoskeletal structures. Electrophoretic analyses have shown that unidentified protein bands of 68,000, 55,000, and 48-50,000 daltons are also present in larger amounts after thrombin stimulation. Since these molecular weights correspond roughly to those of the α, β, and γ chains of fibrin, and since fibrinogen is found in platelet α-granules, these bands were compared to those obtained when purified fibrinogen was treated with thrombin, exposed to 1% Triton X-100-5 mM EGTA, and the resultant Triton-insoluble residue sedimented. Identification of the 68,000-, 55,000-, and 48--50,000-dalton bands as fibrinogen derivatives was confirmed by identifying them in comigration studies and in autoradiographs of Triton-insoluble residues of platelets that were electrophoretically transferred to nitrocellulose paper and treated with antifibrinogen antibody and 125I-protein A. Furthermore, if the platelet suspension was treated with thrombin in the presence of calcium ions, protein bands characteristic of the action of Factor XIII on fibrin were observed, active platelet Factor XIII apparently having been made available by lysis of platelets during preparation. Making use of the electrophoretic properties of tubulin recently described by Best et al [1981], comigration studies using hog brain tubulin indicated that tubulin is not present in significant amounts in the Triton-insoluble residue of platelets as previously suggested. The identification of these proteins as fibrinogen derivatives does not demonstrate a physiological interaction between fibrin and the platelet cytoskeleton, since fibrin is Tritoninsoluble and can be pelleted even in the absence of platelet cytoskeletons.
    Zusätzliches Material: 4 Ill.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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