Atomic force microscopy of thermally treated myosin filaments.
Heat-induced morphological change in myosin filaments was observed using atomic force microscope. The thickness of fixed native myosin filament was estimated to be 95 +/- 5 nm. When myosin filaments in 0.1 M NaCl at pH 6.0 were heated at 40, 55, and 70 degrees C for 10 min, the particulate structure appeared spirally on the surface of the filament at 40 degrees C, and the thickness of the filament was 75 +/- 10 nm. When myosin filaments were treated at 55 degrees C, several filaments were formed associated with side-by-side interaction through projected myosin heads to form a strand. The surface of the strand looked knobby. The thickness of thermally denatured filaments at 55 degrees C was 48 +/- 5 nm, and that of strands was about 80-110 nm, indicating the involvement of several filaments in a strand. The strands became to be rope-like at 70 degrees C, and the individual filaments in a strand were not distinguishable.
Iwasaki
Tomohito
T
Department of Food Science, Rakuno Gakuen University, Ebetsu, Hokkaido 069-8501, Japan. iwasaki@rakuno.ac.jp
Washio
Masahiro
M
Yamamoto
Katsuhiro
K
D000818:Animals; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D018625:Microscopy, Atomic Force; D018482:Muscle, Skeletal / Q000737:chemistry; D009218:Myosins / Q000737:chemistry* / Q000648:ultrastructure*; D011489:Protein Denaturation; D011817:Rabbits; D012965:Sodium Chloride
D012965:Sodium Chloride; D009218:Myosins