The presence of protein phosphokinase activity in a purified nuclear-membrane preparation from adult rat liver was demonstrated by measuring the incorporation of 32P from γ-32P-ATP into endogenous nuclear-membrane proteins as well as into the exogenous protein substrates, dephosphophosvitin (DPV) and lysine-rich histone (LRH). The activity of this enzyme toward DPV was 60 times greater than that toward LRH. cAMP and cGMP did not appear to affect the phosphorylation of endogenous-membrane proteins.
|Original language||English (US)|
|Number of pages||4|
|Journal||Experimental Cell Research|
|State||Published - Mar 15 1979|
Bibliographical noteFunding Information:
This study was supported by grants from the Swedish Medical Research Council No. 04480 and 02235.