Phosphoprotein kinases associated with rat liver chromatin
Two protein kinases associated with rat liver chromatin catalyze the phosphorylation of each specific seryl and threonyl residues of nuclear non-histone proteins. The phosphate acceptor proteins contain a significant quantity of phosphate, and are separated from the enzymes by chromatography on a ph...
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1971 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
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| Übergeordnetes Werk: |
in: Biochemical and Biophysical Research Communications - Amsterdam : Elsevier, 42(1971), 1, Seite 103-110 |
| Übergeordnetes Werk: |
volume:42 ; year:1971 ; number:1 ; pages:103-110 |
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| 520 | |a Two protein kinases associated with rat liver chromatin catalyze the phosphorylation of each specific seryl and threonyl residues of nuclear non-histone proteins. The phosphate acceptor proteins contain a significant quantity of phosphate, and are separated from the enzymes by chromatography on a phospho-cellulose column. Casein and phosvitin also serve as phosphate acceptors. The enzymes show closely similar properties, but were clearly distinguished each other by substrate specificities. With casein as a model substrate one phosphorylated mainly seryl residues, whereas the other preferentially threonyl residues. | ||
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(DE-627)NLEJ184210666 (DE-599)GBVNLZ184210666 DE-627 ger DE-627 rakwb eng Phosphoprotein kinases associated with rat liver chromatin 1971 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Two protein kinases associated with rat liver chromatin catalyze the phosphorylation of each specific seryl and threonyl residues of nuclear non-histone proteins. The phosphate acceptor proteins contain a significant quantity of phosphate, and are separated from the enzymes by chromatography on a phospho-cellulose column. Casein and phosvitin also serve as phosphate acceptors. The enzymes show closely similar properties, but were clearly distinguished each other by substrate specificities. With casein as a model substrate one phosphorylated mainly seryl residues, whereas the other preferentially threonyl residues. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Takeda, M. oth Yamamura, H. oth Ohga, Y. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 42(1971), 1, Seite 103-110 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:42 year:1971 number:1 pages:103-110 http://dx.doi.org/10.1016/0006-291X(71)90368-8 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 42 1971 1 103-110 |
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(DE-627)NLEJ184210666 (DE-599)GBVNLZ184210666 DE-627 ger DE-627 rakwb eng Phosphoprotein kinases associated with rat liver chromatin 1971 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Two protein kinases associated with rat liver chromatin catalyze the phosphorylation of each specific seryl and threonyl residues of nuclear non-histone proteins. The phosphate acceptor proteins contain a significant quantity of phosphate, and are separated from the enzymes by chromatography on a phospho-cellulose column. Casein and phosvitin also serve as phosphate acceptors. The enzymes show closely similar properties, but were clearly distinguished each other by substrate specificities. With casein as a model substrate one phosphorylated mainly seryl residues, whereas the other preferentially threonyl residues. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Takeda, M. oth Yamamura, H. oth Ohga, Y. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 42(1971), 1, Seite 103-110 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:42 year:1971 number:1 pages:103-110 http://dx.doi.org/10.1016/0006-291X(71)90368-8 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 42 1971 1 103-110 |
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(DE-627)NLEJ184210666 (DE-599)GBVNLZ184210666 DE-627 ger DE-627 rakwb eng Phosphoprotein kinases associated with rat liver chromatin 1971 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Two protein kinases associated with rat liver chromatin catalyze the phosphorylation of each specific seryl and threonyl residues of nuclear non-histone proteins. The phosphate acceptor proteins contain a significant quantity of phosphate, and are separated from the enzymes by chromatography on a phospho-cellulose column. Casein and phosvitin also serve as phosphate acceptors. The enzymes show closely similar properties, but were clearly distinguished each other by substrate specificities. With casein as a model substrate one phosphorylated mainly seryl residues, whereas the other preferentially threonyl residues. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Takeda, M. oth Yamamura, H. oth Ohga, Y. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 42(1971), 1, Seite 103-110 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:42 year:1971 number:1 pages:103-110 http://dx.doi.org/10.1016/0006-291X(71)90368-8 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 42 1971 1 103-110 |
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(DE-627)NLEJ184210666 (DE-599)GBVNLZ184210666 DE-627 ger DE-627 rakwb eng Phosphoprotein kinases associated with rat liver chromatin 1971 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Two protein kinases associated with rat liver chromatin catalyze the phosphorylation of each specific seryl and threonyl residues of nuclear non-histone proteins. The phosphate acceptor proteins contain a significant quantity of phosphate, and are separated from the enzymes by chromatography on a phospho-cellulose column. Casein and phosvitin also serve as phosphate acceptors. The enzymes show closely similar properties, but were clearly distinguished each other by substrate specificities. With casein as a model substrate one phosphorylated mainly seryl residues, whereas the other preferentially threonyl residues. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Takeda, M. oth Yamamura, H. oth Ohga, Y. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 42(1971), 1, Seite 103-110 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:42 year:1971 number:1 pages:103-110 http://dx.doi.org/10.1016/0006-291X(71)90368-8 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 42 1971 1 103-110 |
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(DE-627)NLEJ184210666 (DE-599)GBVNLZ184210666 DE-627 ger DE-627 rakwb eng Phosphoprotein kinases associated with rat liver chromatin 1971 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Two protein kinases associated with rat liver chromatin catalyze the phosphorylation of each specific seryl and threonyl residues of nuclear non-histone proteins. The phosphate acceptor proteins contain a significant quantity of phosphate, and are separated from the enzymes by chromatography on a phospho-cellulose column. Casein and phosvitin also serve as phosphate acceptors. The enzymes show closely similar properties, but were clearly distinguished each other by substrate specificities. With casein as a model substrate one phosphorylated mainly seryl residues, whereas the other preferentially threonyl residues. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Takeda, M. oth Yamamura, H. oth Ohga, Y. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 42(1971), 1, Seite 103-110 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:42 year:1971 number:1 pages:103-110 http://dx.doi.org/10.1016/0006-291X(71)90368-8 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 42 1971 1 103-110 |
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Two protein kinases associated with rat liver chromatin catalyze the phosphorylation of each specific seryl and threonyl residues of nuclear non-histone proteins. The phosphate acceptor proteins contain a significant quantity of phosphate, and are separated from the enzymes by chromatography on a phospho-cellulose column. Casein and phosvitin also serve as phosphate acceptors. The enzymes show closely similar properties, but were clearly distinguished each other by substrate specificities. With casein as a model substrate one phosphorylated mainly seryl residues, whereas the other preferentially threonyl residues. |
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Two protein kinases associated with rat liver chromatin catalyze the phosphorylation of each specific seryl and threonyl residues of nuclear non-histone proteins. The phosphate acceptor proteins contain a significant quantity of phosphate, and are separated from the enzymes by chromatography on a phospho-cellulose column. Casein and phosvitin also serve as phosphate acceptors. The enzymes show closely similar properties, but were clearly distinguished each other by substrate specificities. With casein as a model substrate one phosphorylated mainly seryl residues, whereas the other preferentially threonyl residues. |
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Two protein kinases associated with rat liver chromatin catalyze the phosphorylation of each specific seryl and threonyl residues of nuclear non-histone proteins. The phosphate acceptor proteins contain a significant quantity of phosphate, and are separated from the enzymes by chromatography on a phospho-cellulose column. Casein and phosvitin also serve as phosphate acceptors. The enzymes show closely similar properties, but were clearly distinguished each other by substrate specificities. With casein as a model substrate one phosphorylated mainly seryl residues, whereas the other preferentially threonyl residues. |
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