Purification of glycogen phosphorylase by affinity chromatography on 5'-AMP Sepharose.

@article{Sorensen1975PurificationOG,
  title={Purification of glycogen phosphorylase by affinity chromatography on 5'-AMP Sepharose.},
  author={N B Sorensen and P Wang},
  journal={Biochemical and biophysical research communications},
  year={1975},
  volume={67 3},
  pages={
          883-7
        }
}
  • N. B. SorensenP. Wang
  • Published 1 December 1975
  • Biology
  • Biochemical and biophysical research communications
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24 Citations
Highly Influential Citations
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Background Citations
1
Methods Citations
3

24 Citations

Isolation of heart specific isophosphorylase by affinity chromatography on 5'-AMP Sepharose from pig heart.

Determination of phosphorylase kinase activity in crude homogenates by affinity chromatography on 5'-AMP sepharose.

Interaction of ligands with glycogen phosphorylase as revealed by affinity chromatography.

Purification and characterization of glycogen phosphorylase from Drosophila melanogaster

Isolation and partial characterization of two forms of rat heart glycogen phosphorylase.

Rabbit-liver phosphorylase: improvement of the purification procedure and assay of the inactive b form.

Effect of metabolites and phosphorylase on the D to I conversion of glycogen synthase from human polymorphonuclear leukocytes.

Purification and characterization of glycogen phosphorylases from abdominal muscle, heart and integument of the crayfish, Orconectes limosus

Properties and functions of the storage sites of glycogen phosphorylase.

It is demonstrated that the GP catalytic sites are active even in the presence of CDs, and that the actions of the catalytic site and the storage site are independent of each other.

Phosphorylation of glycogen synthase I from human polymorphonuclear leukocytes

  • H. Juhl
  • Biology, Chemistry
    Molecular and Cellular Biochemistry
  • 2006
Glycogen synthase I from human polymorphonuclear leukocytes was phosphorylated with cAMP dependent protein kinase, synthase kinase or phosvitin kinase prepared from these cells, with results concluded that the initial kinetic changes were dependent on phosphorylation of c-A, which contained two sites, one for each kinase.

11 References

A rapid method for the purification of glycogen synthetase I and D utilising concanavalin A bound to agarose.

  • H. SøllingP. Wang
  • Biology, Chemistry
    Biochemical and biophysical research communications
  • 1973

A new assay of phosphorylase based on the filter paper technique.

Enzymes regulating glycogen metabolism in swine subcutaneous adipose tissue. I. Phosphorylase and phosphorylase phosphatase.

Several lines of evidence suggest that AMP inhibition was due to an action on the substrate rather than on the enzyme, suggesting that phosphorylase kinase in homogenates of swine adipose tissue is present largely in an activated form.

The interaction of liver phosphorylase a with glucose and AMP.

Results indicate that the stimulation of the phosphorylase phosphatase reaction by glucose is secondary to the binding of the hexose to phosphorus a, and that this binding is modulated by the concentration of AMP.

Immobilization of glycogen phosphorylase b in its active conformation on matrices substituted with an AMP‐analogue

A rapid filter paper assay for UDPglucose-glycogen glucosyltransferase, including an improved biosynthesis of UDP-14C-glucose.

Glycogen phosphorylase and its converter enzymes in haemolysates of normal human subjects and of patients with type VI glycogen-storage disease. A study of phosphorylase kinase deficiency.

The activity of phosphorylase kinase was measured in haemolysates obtained from a series of patients who had been classified as suffering from type VI glycogenosis, with an almost complete deficiency of phosphate kinase observed in the haEMolysate and in the liver.

A rapid micro assay method for amylo-1,6-glucosidase.

A rapid, sensitive, and specific method for the determination of protein in dilute solution.

Protein measurement with the Folin phenol reagent.