Cyclic 3'5'AMP-stimulated and non-stimulated phosphorylation of protein fractions from rat-liver cell sap on incubation with (γ32p)ATP

Olle Ljungström, Lars Berglund, Gunilla Hjelmquist, Elisabeth Humble, Lorentz Engström

Research output: Contribution to journalArticle

11 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)129-137
Number of pages9
JournalUpsala Journal of Medical Sciences
Volume79
Issue number3
DOIs
StatePublished - 1974
Externally publishedYes

Fingerprint

Adenosine Monophosphate
Adenosine Triphosphate
Phosphorylation
Liver
Proteins
Phosphates
Phosphorylase Kinase
DEAE-Cellulose
Glycogen Synthase
Phosphorylases
Ammonium Sulfate
Detergents
Protein Kinases
Polyacrylamide Gel Electrophoresis
Molecular Weight
Enzymes

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 journalArticle

Ljungström, Olle ; Berglund, Lars ; Hjelmquist, Gunilla ; Humble, Elisabeth ; Engström, Lorentz. / Cyclic 3'5'AMP-stimulated and non-stimulated phosphorylation of protein fractions from rat-liver cell sap on incubation with (γ32p)ATP. In: Upsala Journal of Medical Sciences. 1974 ; Vol. 79, No. 3. pp. 129-137.
@article{23b757d2830f49a2949cb49629a64567,
title = "Cyclic 3'5'AMP-stimulated and non-stimulated phosphorylation of protein fractions from rat-liver cell sap on incubation with (γ32p)ATP",
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.",
author = "Olle Ljungstr{\"o}m and Lars Berglund and Gunilla Hjelmquist and Elisabeth Humble and Lorentz Engstr{\"o}m",
year = "1974",
doi = "10.3109/03009737409178393",
language = "English (US)",
volume = "79",
pages = "129--137",
journal = "Upsala Journal of Medical Sciences",
issn = "0300-9734",
publisher = "Informa Healthcare",
number = "3",

}

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 -