[Contractile proteins in the fractions of soluble and insoluble chromatin of liver and thymus].
The proteins corresponding in molecular weight and solubility in salt solutions to skeletal muscle actin and myosin were revealed in liver and thymus chromatin fragments. When the ionic strength reached 0.3, about 60% of the myosin-like protein identified by electrophoretic mobility of high chains and the K+-EDTA-ATPase activity was cosedimented with nucleohistones. In the presence of ATP or PPi and Mg2+ the solubility of myosin in such salt solutions increased up to 90%, which was paralleled with significant stimulation of RNA release from the nucleohistones. The conformity in the degree of extraction and sedimentation of RNA and intranuclear myosin was also observed in other solutions used during myosin purification. The supposition that the nuclear system of contractile proteins causes labile, ATP-dependent binding of RNA to chromatin is discussed. No essential differences in the actin or myosin contents in the fractions of soluble and non-soluble chromatin were detected.
D000251:Adenosine Triphosphatases / Q000302:isolation & purification; D000818:Animals; D002417:Cattle; D002843:Chromatin / Q000032:analysis*; D003285:Contractile Proteins / Q000302:isolation & purification*; D006657:Histones / Q000302:isolation & purification; D008099:Liver / Q000032:analysis*; D008970:Molecular Weight; D009994:Osmolar Concentration; D051381:Rats; D012995:Solubility; D013950:Thymus Gland / Q000032:analysis*
D002843:Chromatin; D003285:Contractile Proteins; D006657:Histones; D000251:Adenosine Triphosphatases; C026049:EDTA-ATPase
Sokratitel'nye belki v sostave rastvorimogo i ostatochnogo khromatinA pecheni i timusa.