Length of myosin rod and its proteolytic fragments determined by electron microscopy
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چکیده
منابع مشابه
Studies of myosin and its proteolytic fragments by laser Raman spectroscopy.
Two bands in the Raman spectrum of myosin, at 1,304 cm-1 and 1,270 cm-1, are attributable to alpha-helical structure. The first of these, also present in the spectrum of light meromyosin (LMM) but not in that of subfragment-1 (S-1), is assigned to the coiled-coil tail region of myosin; the second, seen in spectra of S-1 or heavy meromyosin (HMM), is largely absent from the spectrum of light mer...
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متن کاملPyrophosphate Binding to and Adenosine Triphosphatase Activity of Myosin and Its Proteolytic Fragments
The binding of pyrophosphate to myosin, heavy meromyosin, and Subfragment 1 was studied by an equilibrium dialysis technique. Myosin binds approximately 2 (1.82) moles/5 X lo5 g of protein, K = 2.07 X 10”. Identical results were obtained with myosin prepared by the ammonium sulfate precipitation procedure with or without LiCl and the dilution method. Red and white skeletal muscle myosin bound t...
متن کاملPyrophosphate binding to and adenosine triphosphatase activity of myosin and its proteolytic fragments. Implications for the substructure of myosin.
The binding of pyrophosphate to myosin, heavy meromyosin, and Subfragment 1 was studied by an equilibrium dialysis technique. Myosin binds approximately 2 (1.82) moles/5 X lo5 g of protein, K = 2.07 X 10”. Identical results were obtained with myosin prepared by the ammonium sulfate precipitation procedure with or without LiCl and the dilution method. Red and white skeletal muscle myosin bound t...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1984
ISSN: 0014-5793
DOI: 10.1016/0014-5793(84)80209-4