Abstract
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) |
|---|---|
| Pages (from-to) | 403-406 |
| Number of pages | 4 |
| Journal | Experimental Cell Research |
| Volume | 119 |
| Issue number | 2 |
| DOIs | |
| State | Published - Mar 15 1979 |
Bibliographical note
Funding Information:This study was supported by grants from the Swedish Medical Research Council No. 04480 and 02235.
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