An electron microscope study of canine cardiac myosin and some of its aggregates.
The morphology of the canine cardiac myosin molecule has been investigated in the electron microscope with Hall's mica-replica technique. The molecule is an elongated rod (shaft) of nonuniform diameter with a globular expansion (head) on one end. Statistical analysis of the lengths of 1908 molecules showed that the mean length was 1610 +/- 250 A; the mean length of the head was 210 +/- 20 A; and the diameter of the head and that of the shaft were 35 to 40 and 15 to 20 A, respectively. About one-third of the molecules had single or multiple, fairly sharp, angulations along their shafts. Rarely, some details of the substructure of the molecule have been observed. Large, spindle-shaped aggregates, measuring 0.5 to 1 micro in length and 50 to 100 A in diameter, were produced by dilution of the myosin solutions. These aggregates were readily visualized in the electron microscope by means of Huxley's negative-staining technique. Projections often were visible along the length of the aggregates except at a central zone where they were frequently absent. The aggregates resembled the thick myofilaments of the myocardium and appeared similar to those produced by Huxley from skeletal myosin solutions.
D000818:Animals; D004285:Dogs; D008854:Microscopy, Electron; D009124:Muscle Proteins / Q000032:analysis*; D009206:Myocardium / Q000032:analysis*; D014461:Ultracentrifugation
D009124:Muscle Proteins