Electron microscopic observations on the interaction of the myosin head subunit with actin in myofibrils.
Glycerol-extracted rabbit psoas muscle fibres were treated with a solution containing the head subunits of myosin. Interaction of the isolated myosin heads with actin filaments in situ was indicated by an increase in the density of the I-band and by an increased diameter of actin filaments alongside their whole length. We conclude that actin filaments are able to interact with a considerably larger number of myosin molecules than that available in the myofibril under in vivo conditions.
D000199:Actins; D000818:Animals; D008854:Microscopy, Electron; D008858:Microscopy, Phase-Contrast; D009132:Muscles; D009210:Myofibrils / Q000648:ultrastructure*; D009218:Myosins; D011487:Protein Conformation; D011817:Rabbits
D000199:Actins; D009218:Myosins