Isolation and characterization of myosin from cloned mouse fibroblasts.
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.
D000199:Actins / Q000378:metabolism; D000251:Adenosine Triphosphatases / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D002850:Chromatography, Gel; D002999:Clone Cells; D004492:Edetic Acid; D004591:Electrophoresis, Polyacrylamide Gel; D005347:Fibroblasts / Q000032:analysis*; D051379:Mice; D008854:Microscopy, Electron; D008970:Molecular Weight; D009218:Myosins / Q000302:isolation & purification* / Q000378:metabolism; D011188:Potassium / Q000378:metabolism; D011485:Protein Binding
D000199:Actins; D000255:Adenosine Triphosphate; D004492:Edetic Acid; D000251:Adenosine Triphosphatases; D009218:Myosins; D011188:Potassium