Interactions of the inhibitory component of troponin, F-actin, and tropomyosin.
The interaction of the inhibitory component (TN I) of troponin and F-actin in  the presence and absence of tropomyosin was studied by a number of physico-chemical techniques: i.e., gel filtration, ultracentrifugation, flow birefringence, viscosity and dynamic viscoelasticity measurements, and electron microscopy.  The results indicated that TN I and F-actin interact with each other more strongly in the presence of tropomyosin than in its absence.  The physiological implication of this finding is discussed.
D000199:Actins / Q000378:metabolism*; D000818:Animals; D001718:Birefringence; D002850:Chromatography, Gel; D004548:Elasticity; D008854:Microscopy, Electron; D009124:Muscle Proteins / Q000378:metabolism*; D009132:Muscles / Q000032:analysis; D011817:Rabbits; D014335:Tropomyosin / Q000378:metabolism*; D014336:Troponin / Q000378:metabolism*; D014461:Ultracentrifugation; D014783:Viscosity
D000199:Actins; D009124:Muscle Proteins; D014335:Tropomyosin; D014336:Troponin