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Myosin Rod Hypophosphorylation and CB Kinetics in Papillary Muscles from a TnC-A8V KI Mouse Model. [PDF]
Biophys J, 2017 Kawai M +5 more
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Electric birefringence of myosin subfragments
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1975Electric birefringence measurements have been made on aqueous solutions of myosin subfragments, heavy meromyosin, subfragments 1 and 2 (S-1 and S-2). All of these showed positive electric birefringence. Heavy meromyosin and S-2 showed a large intrinsic Kerr constant.
Tsuyoshi Totsuka, Syoyu Kobayasi
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Homogeneity of myosin subfragments by equilibrium centrifugation
Biochemistry, 1981A number of enzymes are currently in use for obtaining proteolytic subfragments of rabbit skeletal muscle myosin. Subfragment-1 can be obtained by papain digestion of polymeric myosin in the presence (Mg-S1) or absence (EDTA-S1) of divalent cations [Margossian, S.S., Lowey, S., & Barshop, B. (1975) Nature (London) 258, 163-166].
Susan Lowey +2 more
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Photocleavage of myosin subfragment 1 by vanadate
Biochemistry, 1990The heavy chain of myosin's subfragment 1 (S1) was cleaved at two distinct sites (termed V1 and V2) after irradiation with UV light in the presence of millimolar concentrations of vanadate and in the absence of nucleotides or divalent metals. The V1 site cleavage appeared to be identical with the previously described active site cleavage at serine-180,
Greg T. Long +2 more
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The interdomain motions in myosin subfragment 1
Biophysical Chemistry, 2001The interdomain motions in myosin subfragment 1 (S1) were studied by steady-state and time-resolved fluorescence of tryptophan residues and N-(iodoacetyl)-N'-(5-sulfo-1-naphtyl)ethylenediamine (AEDANS) attached to Cys178 of alkali light chain 1 (A1) exchanged into S1.
Yana K. Reshetnyak, Oleg A. Andreev
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Interaction of globular actin with myosin subfragments
Journal of Molecular Biology, 1971Abstract We have attached a spin label or a fluorescent dye to actin to probe the interaction of G-actin with myosin subfragments. The spin label spectra, which are sensitive to the polymerization of the actin, showed that when heavy meromyosin was added to G-actin the actin was polymerized.
Manuel F. Morales, Roger Cooke
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Interaction of myosin subfragments with F-actin
Biochemistry, 1978The effect of ionic strength, temperature, and divalent cations on the association of myosin with actin was determined in the ultracentrifuge using scanning absorption optics. The association constant (Ka) for the binding of heavy meromyosin (HmM) to F-actin was 1 X 10(7) M-1 at 20 degrees C, in 0.10 M KCl, 0.01 M imidazole (pH 7.0), 5 MM potassium ...
Sarkis S. Margossian, Susan Lowey
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Binding of Myosin Subfragment 1 to Actin
Journal of Biochemistry, 1996The dissociation constant for the binding of myosin subfragment 1 (S1) and chromatographed actin in the presence and absence of nucleotide was measured at various ionic strengths and various temperatures. The dissociation constant was of nM order in the absence of nucleotide and increased by approximately 100- and approximately 100,000-fold in the ...
Fumi Morita, Tsuyoshi Katoh
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Proteolytic separation of an enzymic active subfragment from the myosin-subfragment (S-1)
Biochemical and Biophysical Research Communications, 1967Abstract Direct visualization of myosin molecule by electron microscopy has shown it to be a long rod with a globular head at one end (Rice 1961 Huxley 1963). The use of proteolytic enzymes such as trypsin and chymotrypsin can cleave myosin into well defined and high molecular weight fragments, heavy and light meromyosins (Szent-Gyorgyi 1953 Gergely ...
Yoichi Yazawa +2 more
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