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. 1975 Jul;78(1):93-103.

ATPase activity and filament formation of partially purified myosin from leucocytes

  • PMID: 127790
Free article

ATPase activity and filament formation of partially purified myosin from leucocytes

K Takeuchi et al. J Biochem. 1975 Jul.
Free article

Abstract

Myosin was isolated from leucocytes in horse arterial blood by the same procedures used for the isolation of myosin from skeletal muscle. The Ca2+-, EDTA-, and Mg2+-ATPase [EC 3.6.1.3] activities of the protein was 0.148, 0.147, and 0.001 mumoles/min/mg, respectively, in 0.5 M KCl at pH 7.0 and 25 degrees. The Ca2+-ATPase activity decreased with decrease in the ionic strength. No difference was found between leucocyte myosin and skeletal myosin in the pH profiles of Ca2+- and EDTA-ATPases. The rate and amount of the initial burst of Pi liberation of leucocyte myosin were 0.002 mumoles/min/mg and 0.83 moles/4.8 X 10(5)g, respectively. Leucocyte myosin aggregated into filaments of 0.3 mum length and 150 A diameter, which had a bare shaft and irregular projections. At high ionic strength, the protein bound to skeletal muscle F-actin to form a complex with the characteristic arrowhead structure.

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