Results 121 to 130 of about 20,871 (172)

Interaction between glycogen and glycogen phosphorylase of Tetrahymena

Archives of Biochemistry and Biophysics, 1971
Abstract 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.
V, Kahn, J J, Blum
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A titrimetric assay for glycogen phosphorylase

Analytical Biochemistry, 1973
Abstract 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, A, Lukton
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The Prototype of Glycogen Phosphorylase

Mini-Reviews in Medicinal Chemistry, 2010
The 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 ...
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Protein dynamics of glycogen phosphorylase

Biochemistry, 1986
The 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.
S M, Martin, J R, Lindroth, J W, Ledbetter   +2 more
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A semicontinuous assay for glycogen phosphorylase

Analytical Biochemistry, 1978
Abstract 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.
I T, Carney, R J, Beynon, J, Kay, N, Birket   +3 more
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Catalytic mechanism of glycogen phosphorylase

Faraday Discussions, 1992
Proposals 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 ...
L N, Johnson, S H, Hu, D, Barford
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Interaction of calmodulin and glycogen phosphorylase

Biochimica et Biophysica Acta (BBA) - General Subjects, 1983
We 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.
C, Villar-Palasi, D L, Oshiro, R H, Kretsinger   +2 more
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An automated assay for glycogen phosphorylase

Analytical Biochemistry, 1972
Abstract 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.
R H, Haschke, L M, Heilmeyer
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The allosteric transition of glycogen phosphorylase

Nature, 1989
The 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
D, Barford, L N, Johnson
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Glycogen phosphorylase of Neurospora crassa

Archives of Biochemistry and Biophysics, 1969
Abstract 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.
D, Shepherd, I H, Segel
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