Results 201 to 210 of about 128,949 (267)
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The interaction of muscle glycogen phosphorylase b with glycogen
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982Interaction of muscle glycogen phosphorylase b (EC 2.4.1.1) with glycogen was studied by sedimentation, stopped-flow and temperature-jump methods. The equilibrium enzyme concentration was determined by sedimentation in an analytical ultracentrifuge equipped with absorption optics and a photoelectric scanning system.
N.P. Lissovskaya +4 more
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A semicontinuous assay for glycogen phosphorylase
Analytical Biochemistry, 1978Abstract An assay for phosphorylase a or b is described in which the rate of release of phosphate from glucose 1-phosphate is followed by means of an “instantaneous” method for determination of phosphate.
Robert J. Beynon +3 more
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Interaction between glycogen and glycogen phosphorylase of Tetrahymena
Archives of Biochemistry and Biophysics, 1971Abstract The glycogen phosphorylase of Tetrahymena pyriformis complexes with glycogen as judged by its elution pattern from columns of Sepharose 6B. Complex formation does not occur with starch, amylose, or amylopectin, and neither do these polyglucans serve as primers for the enzyme.
Varda Kahn, Jacob J. Blum
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The allosteric transition of glycogen phosphorylase
Nature, 1989The crystal structure of R-state glycogen phosphorylase b has been determined at 2.9 A resolution. A comparison of T-state and R-state structures of the enzyme explains its cooperative behaviour on ligand binding and the allosteric regulation of its activity. Communication between catalytic sites of the dimer is provided by a change in packing geometry
Louise N. Johnson, David Barford
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An automated assay for glycogen phosphorylase
Analytical Biochemistry, 1972Abstract An automated assay of glycogen phosphorylase based on the method of Hedrick and Fischer (6) was developed using the Technicon Auto-Analyzer system. Since a protein precipitate is formed when measuring the product (inorganic phosphate), a dialysis step is commonly employed.
Ludwig M. G. Heilmeyer +1 more
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Evolution of Allosteric Control in Glycogen Phosphorylase
Journal of Molecular Biology, 1993In relation to the primary sequence and three-dimensional structure of rabbit muscle glycogen phosphorylase, we have carried out a comparative sequence analysis of phosphorylases from human, rat, Dictyostelium, yeast, potato and Escherichia coli. Based on sequence similarity, a large region of the protein is shared by these enzymes extending from alpha-
Hudson, J. W. +2 more
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Fish muscle glycogen phosphorylase
Canadian Journal of Biochemistry, 1968Glycogen phosphorylase b was purified 70- to 90-fold from skeletal muscle of rainbow trout (Salmo gairdneri). The purified enzyme exhibited maximal activity near pH 6.8 at 37°. Of several 5′-nucleotides tested, only 5′-AMP caused stimulation of phosphorylase b. The Km value for glucose-1-phosphate was 10–15 mM, and for 5′-AMP, 0.2–0.4 mM.
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Genetic deficiencies of the glycogen phosphorylase system
Human Genetics, 1996Several types of glycogen storage disease attributable to a deficiency of phosphorylase or phosphorylase kinase have been described. These diseases have been divided according to clinical symptoms, mode of inheritance, and affected tissue. However, this classification is questionable, as the clinical symptoms of these different diseases are similar ...
Patrick Willems, Jan Hendrickx
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On the activities of glycogen phosphorylase and glycogen synthase in the liver of the rat
Biochimica et Biophysica Acta (BBA) - General Subjects, 1978A procedure was developed for determination of glycogen synthase and phosphorylase activities in liver after various in vivo physiological treatments. Liver samples were obtained from anaesthetised rats by freeze-clamping in situ. Other procedures were shown to stimulate the activity of phosphorylase and depress the activity of glycogen in the liver ...
J.McD. Armstrong, Julie D. Newman
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THE EFFECT OF THIOPENTAL ON HEPATIC GLYCOGEN PHOSPHORYLASE
The Journal of Pharmacology and Experimental Therapeutics, 1965The effect of thiopental on glycogen phosphorylase activity of liver and diaphragm was studied in vitro . Thiopental was found to cause an increase in active glycogen phosphorylase in liver but not in diaphragm. The thiopentalinduced increase in active phosphorylase in liver was additive with the stimulation produced by epinephrine.
Edward A. Brunner, Niels Haugaard
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