Isolation and Characterization of Myosin from Cloned Mouse Fibroblasts

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 1972 Dec 1

PMID 4264772

Citations 37

Authors

R S Adelstein

M A Conti

G S Johnson

I Pastan

T D Pollard

Affiliations

Soon will be listed here.

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 Mg(2+) in 0.6 M KCl and is activated by rabbit muscle actin in the presence of Mg(2+) 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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