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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1972 Dec;69(12):3693–3697. doi: 10.1073/pnas.69.12.3693

Isolation and Characterization of Myosin from Cloned Mouse Fibroblasts

Robert S Adelstein *, Mary Anne Conti *, George S Johnson , Ira Pastan , Thomas D Pollard
PMCID: PMC389851  PMID: 4264772

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.

Keywords: muscle, SDS-acrylamide gel electrophoresis, actin binding, agarose filtration

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Selected References

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