Isolation and Characterization of Myosin from Cloned Mouse Fibroblasts

  1. Robert S. Adelstein*,
  2. Mary Anne Conti*,
  3. George S. Johnson†,
  4. Ira Pastan†, and
  5. Thomas D. Pollard‡
  1. *Cardiology Branch, National Heart and Lung Institute, Bethesda, Maryland 20014
  2. †Laboratory of Molecular Biology, National Cancer Institute, Bethesda, Md.
  3. ‡Harvard Medical School, Boston, Massachusetts

Abstract

Myosin has been isolated from cloned mouse fibroblasts, line L-929. Fibroblast myosin: (i) binds to rabbit muscle actin and is dissociated from it by ATP, (ii) has an ATPase activity that is suppressed by Mg2+ in 0.6 M KCl and is activated by rabbit muscle actin in the presence of Mg2+ in 14 mM KCl, (iii) forms thin bipolar aggregates in 0.1 M KCl when viewed in the electron microscope, (iv) possesses a heavy chain with the same mobility as muscle myosin (molecular weight 200,000) in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. In these respects, fibroblast myosin appears to be similar to muscle myosin in structure and function.

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  1. PNAS December 1, 1972 vol. 69 no. 12 3693-3697
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