title: Nature of the phosphorylated 26 000 molecular weight protein extracted from dog thyroid with contractile proteins.
abstract: Dog thyroid contractile proteins are characterized by their ATPase activity at high KCl concentration. In the presence of Ca(2+), 80 nmol ATP are hydrolyzed per min per mg protein. This Ca(2+) -ATPase activity is inhibited by Mg(2+) but not influenced by sodium azide. The 26 000 molecular weight protein which is present in thyroid contractile protein preparations and the phosphorylation of which is stimulated by thyroid stimulating hormone (TSH) is suggested to be identical to the lysine-rich histones (H1). Indeed, radioactive thyroid H1 histones added to unlabelled thyroid slices copurify with the contractile proteins and migrate at the same level as the 26 000 molecular weight when submitted to electrophoresis in polyacrylamide sodium dodecyl sulfate gels of different acrylamide concentrations.
mesh_terms: D000818:Animals; D000252:Calcium-Transporting ATPases / Q000378:metabolism; D003285:Contractile Proteins / Q000302:isolation & purification*; D004285:Dogs; D006657:Histones / Q000302:isolation & purification*; D008970:Molecular Weight; D010766:Phosphorylation; D013961:Thyroid Gland / Q000032:analysis*
chemical_list: D003285:Contractile Proteins; D006657:Histones; D000252:Calcium-Transporting ATPases