Abstract
1. 1. We have fractionated and partially purified several rat liver nuclear protein kinases by utilizing endogenous (nonhistone proteins) and exogenous acidic (dephosphophosvitin) and basic (lysinerich histone) protein substrates. 2. 2. Three enzymes were active towards endogenous substrates, two towards dephosphophosvitin and two towards lysine-rich histone. 3. 3. Of the latter only one was cAMP-dependent. however, only minimal cAMP binding activity was detected. 4. 4. Several features of these enzyme reactions are described revealing distinct differences in the characteristics of each of these enzymes.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1109-1118 |
| Number of pages | 10 |
| Journal | International Journal of Biochemistry |
| Volume | 15 |
| Issue number | 9 |
| DOIs | |
| State | Published - 1983 |
Bibliographical note
Funding Information:A~litzttt~tc~tlyen~~~~ãsss-is-tSaknicllee dof MS K. Ferkul and Mr A. T. Davis is gratefully acknowledged. This work aas supported in part by the VA Medical Research Fund and by the PHS research grant No. CA-15062 awarded by NCI, D.H.H.S.