Paramyosin structures in the thick filaments of the anterior byssus retractor muscle of Mytilus edulis.
Freeze-substituted cells of the anterior byssus retractor muscle of Mytilus edulis contain paramyosin filaments which exhibit a characteristic fine structure. Longitudinally sectioned filaments show a variety of band patterns, those occurring most frequently being cross, oblique or double oblique striations. The periodic spacings within one pattern are precise as can be demonstrated by Markham analysis and optical diffractometry. The patterns arise from structures in the interior of the filament since they persist in serially sectioned filaments and a layered structure is visible in cross-sectioned filaments. The different patterns are found to be convertible by rotating the grid around the filament axis. The observations led to the conclusion that the paramyosin core has some kind of helical arrangement. A model is proposed which consists of concentric layers of parallel paramyosin molecules which are displaced along the molecular axis in such a way that the characteristic Bear-Selby net structure results.
D000818:Animals; D049872:Bivalvia / Q000648:ultrastructure*; D005615:Freezing; D008854:Microscopy, Electron / Q000379:methods; D008961:Models, Structural; D009132:Muscles / Q000648:ultrastructure*; D014335:Tropomyosin / Q000502:physiology*
D014335:Tropomyosin