Partly Hypothetical Representation of the Interaction Between Actin and Myosin Myofilaments in Relaxed and Contracted Myofibrils (Modified after HAM 1974 and MOREL and PINSET-HÄRSTRÖM 1975)
The thick myosin myofilaments (Figs. A1, B1) are composed of bipartite, threadlike, approximately 150-nm-long myosin molecules. Light meromyosin (Figs. A2, B2), which is approximately 80 nm long, makes up the actual backbone of myosin myofilaments, whereas heavy meromyosin (Figs. A3, B3) forms shorter sections and terminates in a globular head (Figs. A4, B4).
KeywordsMyosin Head Myosin Filament Globular Head Heavy Meromyosin Hypothetical Representation
- Ham AW (1974) Histology, 7th edn. Lippincott, Philadelphia.Google Scholar
- Huxley HE (1983) Molecular basis of contraction in cross-striated muscles and relevance to motile mechanisms in other cells. In: Stracher A (ed) Muscle and nonmuscle motility, vol 1. Academic, New York.Google Scholar
- Morel JE, Pinset-Härstròm I (1975) Ultrastructure of the contractile system of striated skeletal muscle and the processes of muscular contraction: I. Ultrastructure of the myofibril and source of energy. Biomedicine 22:88–96.Google Scholar
- Pepe FA (1983) Macromolecular assembly of myosin. In: Stracher A (ed) Muscle and nonmuscle motility, vol 1. Academic, New York.Google Scholar