Abstract
Rat-liver cell sap protein was separated into four fractions by pH 5.5 precipitation and ammonium sulfate fractionation. On incubation with (32P)ATP, protein of two of the fractions was phosphorylated, showing the presence of protein kinase activity and endogenous protein substrates. The phosphorylation of one of the fractions was markedly stimulated by cyclic 3'5'AMP. Strong evidence was obtained that this phosphate-incorporating material was neither active phosphorylase, phosphorylase kinase nor glycogen synthetase. The two phosphate-incorporating fractions were chromatographed on DEAE-cellulose with stepwise elution. Several subtractions contained material which was phosphorylated on incubation with (32P)ATP. The phosphorylation of two subfractions was greatly stimulated by cyclic 3'5'AMP. By polyacrylamide gel electrophoresis in detergent of (32P)ATP-incubated material from these fractions, three major 32P-labelled components with estimated molecular weights of 62000, 55000 and 47 000 were demonstrated. It is supposed that these components are derived from enzymes or other proteins with functions regulated by phosphorylation-dephosphorylation reactions.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 129-137 |
| Number of pages | 9 |
| Journal | Upsala Journal of Medical Sciences |
| Volume | 79 |
| Issue number | 3 |
| DOIs | |
| State | Published - 1974 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Medicine(all)
Cite this
Cyclic 3'5'AMP-stimulated and non-stimulated phosphorylation of protein fractions from rat-liver cell sap on incubation with (γ32p)ATP. / Ljungström, Olle; Berglund, Lars; Hjelmquist, Gunilla; Humble, Elisabeth; Engström, Lorentz.
In: Upsala Journal of Medical Sciences, Vol. 79, No. 3, 1974, p. 129-137.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Cyclic 3'5'AMP-stimulated and non-stimulated phosphorylation of protein fractions from rat-liver cell sap on incubation with (γ32p)ATP
AU - Ljungström, Olle
AU - Berglund, Lars
AU - Hjelmquist, Gunilla
AU - Humble, Elisabeth
AU - Engström, Lorentz
PY - 1974
Y1 - 1974
N2 - Rat-liver cell sap protein was separated into four fractions by pH 5.5 precipitation and ammonium sulfate fractionation. On incubation with (32P)ATP, protein of two of the fractions was phosphorylated, showing the presence of protein kinase activity and endogenous protein substrates. The phosphorylation of one of the fractions was markedly stimulated by cyclic 3'5'AMP. Strong evidence was obtained that this phosphate-incorporating material was neither active phosphorylase, phosphorylase kinase nor glycogen synthetase. The two phosphate-incorporating fractions were chromatographed on DEAE-cellulose with stepwise elution. Several subtractions contained material which was phosphorylated on incubation with (32P)ATP. The phosphorylation of two subfractions was greatly stimulated by cyclic 3'5'AMP. By polyacrylamide gel electrophoresis in detergent of (32P)ATP-incubated material from these fractions, three major 32P-labelled components with estimated molecular weights of 62000, 55000 and 47 000 were demonstrated. It is supposed that these components are derived from enzymes or other proteins with functions regulated by phosphorylation-dephosphorylation reactions.
AB - Rat-liver cell sap protein was separated into four fractions by pH 5.5 precipitation and ammonium sulfate fractionation. On incubation with (32P)ATP, protein of two of the fractions was phosphorylated, showing the presence of protein kinase activity and endogenous protein substrates. The phosphorylation of one of the fractions was markedly stimulated by cyclic 3'5'AMP. Strong evidence was obtained that this phosphate-incorporating material was neither active phosphorylase, phosphorylase kinase nor glycogen synthetase. The two phosphate-incorporating fractions were chromatographed on DEAE-cellulose with stepwise elution. Several subtractions contained material which was phosphorylated on incubation with (32P)ATP. The phosphorylation of two subfractions was greatly stimulated by cyclic 3'5'AMP. By polyacrylamide gel electrophoresis in detergent of (32P)ATP-incubated material from these fractions, three major 32P-labelled components with estimated molecular weights of 62000, 55000 and 47 000 were demonstrated. It is supposed that these components are derived from enzymes or other proteins with functions regulated by phosphorylation-dephosphorylation reactions.
UR - http://www.scopus.com/inward/record.url?scp=0016177711&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0016177711&partnerID=8YFLogxK
U2 - 10.3109/03009737409178393
DO - 10.3109/03009737409178393
M3 - Article
C2 - 4372760
AN - SCOPUS:0016177711
VL - 79
SP - 129
EP - 137
JO - Upsala Journal of Medical Sciences
JF - Upsala Journal of Medical Sciences
SN - 0300-9734
IS - 3
ER -