Open AccessIsolation and Characterization of Myosin from Cloned Mouse Fibroblasts
Author(s) -
Robert Adelstein,
Mary Anne Conti,
George S. Johnson,
Ira Pastan,
Thomas D. Pollard
Publication year - 1972
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.69.12.3693
Subject(s) - myosin , actin , sodium dodecyl sulfate , gel electrophoresis , fibroblast , polyacrylamide gel electrophoresis , electron microscope , microbiology and biotechnology , chemistry , biochemistry , myosin light chain kinase , biology , enzyme , in vitro , physics , optics
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.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom