Results 191 to 200 of about 128,949 (267)
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Role of glycogen phosphorylase in liver glycogen metabolism.
Molecular Aspects of Medicine, 2015Liver glycogen is synthesized after a meal in response to an increase in blood glucose concentration in the portal vein and endocrine and neuroendocrine signals, and is degraded to glucose between meals to maintain blood glucose homeostasis. Glycogen degradation and synthesis during the diurnal cycle are mediated by changes in the activities of ...
L. Agius
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The prototype of glycogen phosphorylase.
Mini-Reviews in Medicinal Chemistry, 2010The quest for the discovery of new antihyperglycemic agents has been more intense the last years due to the rapid increase of mortality associated with type 2 diabetes. Glycogen metabolism has been one of the major causes of the elevated blood glucose levels; hence, special attention has been drawn to the control of the enzymes implicated in the ...
E. Chrysina
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Glycogen Phosphorylase Inhibitors
Mini-Reviews in Medicinal Chemistry, 2006Type 2 diabetes is a complex metabolic disease with hyperglycemia as its recognizable hallmark. Hepatic glucose output is elevated in Type 2 diabetic patients, and evidence suggests drugs which lower hepatic glucose production are effective antihyperglycemic agents.
Steven M Sparks, Brad R. Henke
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On the mechanism of glycogen phosphorylase
Archives of Biochemistry and Biophysics, 1972Abstract The rate of exchange of 18 O from the COP position into the external positions of the phosphate group of glucose 1-phosphate was studied. An indirect method, involving acid-catalyzed exchange of 18 O into the 1-position of glucose 6-phosphate followed by isomerization with phosphoglucomutase, was used to prepare a rapidly equilibrating ...
Allen M. Gold, Michael P. Osber
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Archives of Biochemistry and Biophysics, 1964
Abstract Brain glycogen phosphorylase has been shown to exist in an inactive and an active form. The inactive enzyme shows no activity in the absence of AMP but is maximally active in the presence of this nucleotide. The inactive enzyme has been purified 100-fold by adsorption on starch, followed by elution of other protein and finally elution of the
George I. Drummond +2 more
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Abstract Brain glycogen phosphorylase has been shown to exist in an inactive and an active form. The inactive enzyme shows no activity in the absence of AMP but is maximally active in the presence of this nucleotide. The inactive enzyme has been purified 100-fold by adsorption on starch, followed by elution of other protein and finally elution of the
George I. Drummond +2 more
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A titrimetric assay for glycogen phosphorylase
Analytical Biochemistry, 1973Abstract A titrimetric method for the assay of glycogen phosphorylase is presented in which a direct and continuous course of reaction is obtained over a wide range of enzyme concentrations (7.2–378.3 μg/ml). The method resulted in rates which were in agreement with those obtained using the inorganic phosphate method, and the expected value of the ...
K. Palter, Aaron Lukton
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Interaction of calmodulin and glycogen phosphorylase
Biochimica et Biophysica Acta (BBA) - General Subjects, 1983We have demonstrated the interaction of 125I-labeled calmodulin with glycogen phosphorylase by four techniques: polyacrylamide gel overlay, sucrose density centrifugation, gel filtration chromatography, and affinity chromatography. Phosphorylase b has more affinity for calmodulin than does phosphorylase a.
Carlos Villar-Palasi +2 more
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Protein dynamics of glycogen phosphorylase
Biochemistry, 1986The glycogen phosphorylase molecule absorbs the ultraviolet energy of a nitrogen laser to form an excited state of the cofactor. The decay rate of this state has a lifetime of 6.7 microseconds, and its sensitivity to bound substrates presents a new perspective of the mechanism.
John W. Ledbetter +2 more
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Catalytic mechanism of glycogen phosphorylase
Faraday Discussions, 1992Proposals for the catalytic mechanism of glycogen phosphorylase based on crystallographic studies with the T-state form of the enzyme are reviewed in the light of new structural data from studies with the R-state enzyme. The observed position for a sulfate ion at the catalytic site and the crystallographic binding studies of glucose-1-P to the R-state ...
S.-H. Hu, D Barford, L N Johnson
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Glycogen phosphorylase of Neurospora crassa
Archives of Biochemistry and Biophysics, 1969Abstract Glycogen phosphorylase (α-1,4-glucan: orthophosphate glucosyltransferase, EC 2.4.1.1) was purified more than 1300-fold from cell-free extracts of Neurospora crassa . The final preparation, which has a specific activity of 146 units/mg protein, is at least 50% pure as judged by polyacrylamide disc gel electrophoresis.
Irwin H. Segel, David Shepherd
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