Regulation of muscle contraction: bindings of troponin and its components to actin and tropomyosin.
The bindings of troponin components to actin and tropomyosin has been studied by cosedimentation with actin and affinity chromatography. It is shown that troponin binds to actin and tropomyosin in the presence and absence of calcium but the binding to actin is sensitive to ionic strength. Troponin-I + C binds to actin-tropomyosin in the absence of calcium but not to actin or tropomyosin alone. Troponin-I binds to actin and the binding is improved in the presence of tropomyosin even though troponin-I does not bind to tropomyosin alone. Troponin-C does not bind to actin or tropomyosin. The results suggest that the binding of troponin by actin is influenced by tropomyosin. A model of regulation by troponin is proposed.
D000199:Actins / Q000502:physiology*; D000251:Adenosine Triphosphatases / Q000378:metabolism; D000818:Animals; D002645:Chickens; D007700:Kinetics; D046911:Macromolecular Substances; D008954:Models, Biological; D009119:Muscle Contraction; D009124:Muscle Proteins / Q000502:physiology*; D009132:Muscles / Q000502:physiology; D011485:Protein Binding; D014335:Tropomyosin / Q000502:physiology*; D014336:Troponin / Q000502:physiology*
D000199:Actins; D046911:Macromolecular Substances; D009124:Muscle Proteins; D014335:Tropomyosin; D014336:Troponin; D000251:Adenosine Triphosphatases