X-ray diffraction evidence for cross-bridge formation in relaxed muscle fibers at various ionic strengths.
Equatorial x-ray diffraction patterns from single skinned rabbit psoas fibers were studied at various ionic strengths to obtain structural information regarding cross-bridge formation in relaxed muscle fibers. At ionic strengths between 20 and 50 mM, the intensity of the 11 reflection, I11, of the relaxed state was close to that of the rigor state, whereas the intensity of the 10 reflection, I10, was approximately twice that of rigor reflection. Calculations by two-dimensional Fourier synthesis indicated that substantial extra mass was associated with the thin filaments under these conditions. With increasing ionic strength between 20 and 100 mM, I10 increased and I11 decreased in an approximately linear way, indicating net transfer of mass away from the thin filaments towards the thick filaments. These results provided evidence that cross-bridges were formed in a relaxed fiber at low ionic strengths, and that the number of cross-bridges decreased as ionic strength was raised. Above mu = 100 mM, I10 and I11 both decreased, indicating the onset of increasing disorder within the filament lattice.
D000199:Actins; D000205:Actomyosin; D000255:Adenosine Triphosphate; D000818:Animals; D009119:Muscle Contraction; D009126:Muscle Relaxation; D009132:Muscles / Q000648:ultrastructure*; D009218:Myosins; D009994:Osmolar Concentration; D011817:Rabbits; D012518:Sarcomeres / Q000648:ultrastructure; D014961:X-Ray Diffraction
D000199:Actins; D000255:Adenosine Triphosphate; D000205:Actomyosin; D009218:Myosins