P. Ekman

发表

Comparative kinetic studies on the L-type pyruvate kinase from rat liver and the enzyme phosphorylated by cyclic 3', 5'-AMP-stimulated protein kinase.

P. Ekman, U. Dahlqvist, E. Humble, 1976, Biochimica et Biophysica Acta.

Phosphorylation of glucokinase from rat liver in vitro by protein kinase A with a concomitant decrease of its activity.

E. Nilsson, P. Ekman, 1988, Archives of biochemistry and biophysics.

Fructose-1,6-bisphosphatase from rat liver. A comparison of the kinetics of the unphosphorylated enzyme and the enzyme phosphorylated by cyclic AMP-dependent protein kinase.

K. Ekdahl, P. Ekman, 1985, The Journal of biological chemistry.

Quantification of subnanomolar amounts of phosphate bound to seryl and threonyl residues in phosphoproteins using alkaline hydrolysis and malachite green.

P. Ekman, O. Jäger, 1993, Analytical biochemistry.

In vitro phosphorylation of human complement factor C3 by protein kinase A and protein kinase C. Effects on the classical and alternative pathways.

B. Nilsson, U. Nilsson, P. Ekman, 1990, The Journal of biological chemistry.

Dephosporylation with alkaline phosphatase of histone and fibrinogen phosphorylated with protein kinase C in vitro.

P. Ekman, 1991, Upsala journal of medical sciences.

Glucagon-induced phosphorylation of pyruvate kinase (type L) in rat liver slices.

P. Ekman, O. Ljungström, 1977, Biochemical and biophysical research communications.

The quantity of protein-bound [32P]phosphotyrosine in hepatocytes and fibroblasts. The effects of tyrosine protein kinase activating agents.

P. Ekman, L. Engström, B. Ek, 1987, Journal of biochemistry.

Substrate specificity of protein kinase C studied with peptides containing D-amino acid residues.

J. Järv, P. Ekman, L. Engström, 1993, Journal of biochemistry.

Protein kinase C phosphorylates two of the four known syndecan cytoplasmic domains in vitro.

T. Prasthofer, P. Ekman, S. Johansson, 1995, Biochemistry and molecular biology international.

Amino acid sequence at the phosphorylated site of rat liver pyruvate kinase.

P. Ekman, U. Dahlqvist, V. Titanji, 1975, Biochemical and biophysical research communications.

In vitro phosphorylation of serum albumin by two protein kinases: a potential pitfall in protein phosphorylation reactions.

P. Ekman, S. C. Martin, 1986, Analytical biochemistry.

The kinetics of unphosphorylated, phosphorylated and proteolytically modified fructose bisphosphatase from fat liver.

P. Ekman, U. Dahlqvist-Edberg, 1981, Biochimica et biophysica acta.

The effect of fructose 2,6‐bisphosphate and AMP on the activity of phosphorylated and unphosphorylated fructose‐1,6‐bisphosphatase from rat liver

P. Ekman, K. Nilsson Ekdahl, 1984, FEBS letters.

Proteolytic modification of pig and rat liver pyruvate kinase type L including phosphorylatable site.

P. Ekman, E. Humble, L. Engström, 1978, Biochimica et biophysica acta.

Rapid proteolytic removal of phosphopeptides and phosphorylatable sites from proteins in rat liver cell SAP

P. Ekman, L. Engström, G. Bergström, 1978, FEBS letters.

The demonstration in rat liver cell sap of protein kinase and phosphoprotein phosphatase active on fructose-bisphosphatase.

P. Ekman, M. Wretborn, U. Dahlqvist-Edberg, 1982, Biochimica et biophysica acta.

Detection and identification of substrates for protein kinases: use of proteins and synthetic peptides.

P. Ekman, E. Humble, L. Engström, 1984, Methods in enzymology.

Model studies on iron(III) ion affinity chromatography. II. Interaction of immobilized iron(III) ions with phosphorylated amino acids, peptides and proteins.

J. Porath, P. Ekman, G Muszyńska, 1992, Journal of chromatography.

Endogenous substrates of protein kinase in rat liver cell sap under different dietary conditions.

P. Ekman, L. Engström, U. Dahlqvist-Edberg, 1978, Biochimica et biophysica acta.

Purification of a Ca2+-activated protease from rat erythrocytes and its possible effect on pyruvate kinase in vivo.

P. Ekman, U. Dahlqvist-Edberg, 1981, Biochimica et biophysica acta.

Subtilisin‐catalyzed removal of phosphorylated site of pig liver pyruvate kinase without inactivation of the enzyme

P. Ekman, U. Dahlqvist, E. Humble, 1975, FEBS letters.

Phospholipid-dependent and EGTA-inhibited protein kinase from maize seedlings.

P. Ekman, L. Engström, G. Muszyńska, 1993, Biochemistry and molecular biology international.

Endothelial cells release casein kinase II--like activity capable of phosphorylating fibrinogen in response to thrombin.

P. Ekman, S. Eriksson, J. Alston-Smith, 1993, Thrombosis research.

The in vitro modification of phosphorylated pyruvate kinase by a Ca2+-activated protease from rat liver.

P. Ekman, I. Eriksson, 1980, Acta chemica Scandinavica. Series B: Organic chemistry and biochemistry.

A potential pitfall in protein kinase assay: phosphocellulose paper as an unreliable adsorbent of produced phosphopeptides.

P. Ekman, L. Engström, R. Toomik, 1992, Analytical biochemistry.

Substrate specificity studies on protein kinase C

J. Järv, P. Ekman, L. Engström, 1993 .