Ca2+-sensitive transition in the molecular conformation of molluscan muscle myosins.
Filament assemblies of myosin molecules purified from scallop adductor muscles were stabilized by Ca2+ in the presence of ATP or ADP. Electron micrographs showed that the tail part of monomeric myosin molecules was folded in the absence of Ca2+, but was extended in the presence of Ca2+ at physiological ionic strength.
Takahashi
M
M
Department of Chemistry, Faculty of Science, Hokkaido University, Sapporo.
Fukushima
Y
Y
Inoue
K
K
Hasegawa
Y
Y
Morita
F
F
Takahashi
K
K
D000255:Adenosine Triphosphate / Q000032:analysis; D000818:Animals; D049872:Bivalvia; D002118:Calcium / Q000502:physiology*; D008974:Mollusca / Q000378:metabolism*; D009132:Muscles / Q000502:physiology*; D009218:Myosins / Q000502:physiology*; D010766:Phosphorylation; D011487:Protein Conformation; D012995:Solubility
D000255:Adenosine Triphosphate; D009218:Myosins; D002118:Calcium