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  • Title: [Tropomyosin and myosin subfragment 1 induce in thin muscle fiber filaments differing conformational changes in the C-terminal portion of the polypeptide chain of actin].
    Author: Borovikov IuS, Dobrowolski Z, Dabrowska R.
    Journal: Tsitologiia; 1988 Aug; 30(8):1014-7. PubMed ID: 3206540.
    Abstract:
    Muscle fibres, free of myosin, troponin and tropomyosin, containing thin filaments reconstructed from G-actin and modified by fluorescent label 1,5-IAEDANS were used for polarized microfluorimetric studies of the effect of tropomyosin (TM) from smooth muscles, and of subfragment 1 (S1) from skeletal muscles on the structural state of F-actin. TM and S1 were shown to initiate different changes in polarized fluorescence of 1,5-IAEDANS of F-actin: TM increases, whereas S1 decreases fluorescent anisotropy. It was suggested that the structural state of F-actin may differ in the C-terminal of polypeptide chain of actin.
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