Properties of porcine platelet myosin. II. Shape change of the molecule.
Porcine platelet myosin molecules were examined by electron microscopy for changes in their shape. At high ionic strength, the molecules were morphologically indistinguishable from skeletal muscle myosin, except for a slight difference in the bent regions of their tails. At physiological ionic strength, however, the following important difference was observed between the two myosins. Unlike skeletal muscle myosin, the filaments of nonphosphorylated platelet myosin could be disassembled by stoichiometric ATP into a monomeric form with sharply bent or folded tail, and reassembled after ATP hydrolysis. Similar disassembly changes could be induced by various nucleotide triphosphates (CTP, GTP, ITP, and UTP) and to a lesser extent by ADP, AMP, and AMPPNP. These results suggest that ATP binds to the hydrolytic sites in platelet myosin molecule and induces the molecular shape change.
D000255:Adenosine Triphosphate / Q000494:pharmacology; D000818:Animals; D001665:Binding Sites; D001792:Blood Platelets / Q000032:analysis* / Q000648:ultrastructure; D006868:Hydrolysis; D008027:Light; D008854:Microscopy, Electron; D009132:Muscles / Q000032:analysis; D009218:Myosins / Q000097:blood*; D011487:Protein Conformation; D011817:Rabbits; D012542:Scattering, Radiation; D013050:Spectrometry, Fluorescence; D013552:Swine
D000255:Adenosine Triphosphate; D009218:Myosins