Results 171 to 180 of about 76,168 (194)
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The Journal of Nutrition, 1984
Rats were fasted 24, 48 or 72 hours to determine the effect of several days without food on glycogen synthase and synthase phosphatase activity in heart. The basal percentage of synthase I decreased gradually from approximately 20% in fed animals to approximately 6% in rats starved for 72 hours. Glycogen increased progressively from 4.6 mg/g wet weight
Frank Q. Nuttall, Mary C. Gannon
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Rats were fasted 24, 48 or 72 hours to determine the effect of several days without food on glycogen synthase and synthase phosphatase activity in heart. The basal percentage of synthase I decreased gradually from approximately 20% in fed animals to approximately 6% in rats starved for 72 hours. Glycogen increased progressively from 4.6 mg/g wet weight
Frank Q. Nuttall, Mary C. Gannon
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2003
The chapter provides a short summary of the structure, substrate specificity, functions, and regulation of glycogen synthase kinase 3 protein. Glycogen synthase kinase 3 (GSK3) is a protein that phosphorylates and inhibits glycogen synthase, the enzyme that catalyzes the transfer of glucose from UDPG to glycogen.
Cohen, Philip, Frame, Sheelagh
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The chapter provides a short summary of the structure, substrate specificity, functions, and regulation of glycogen synthase kinase 3 protein. Glycogen synthase kinase 3 (GSK3) is a protein that phosphorylates and inhibits glycogen synthase, the enzyme that catalyzes the transfer of glucose from UDPG to glycogen.
Cohen, Philip, Frame, Sheelagh
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Glycogen Synthase and Glycogen Synthase Kinases
1981Publisher Summary This chapter focuses on properties and other biochemical and physiological processes related to glycogen synthase and glycogen synthase kinases. The reversible covalent modification of proteins appears to be one of the fundamental mechanisms that have evolved to regulate the inherent properties of enzyme molecules.
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Phosphorylation of rat liver glycogen synthase bound to the glycogen particle
Archives of Biochemistry and Biophysics, 1984Rat liver glycogen synthase bound to the glycogen particle was partially purified by repeated high-speed centrifugation. This synthase preparation was labeled with 32P by incubations with cAMP-dependent protein kinase and cAMP-independent synthase (casein) kinase-1 in the presence of [gamma-32P]ATP.
Kuo-Ping Huang +2 more
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Electron microscope studies of glycogen synthase
Molecular and Cellular Biochemistry, 1973Glycogen synthase from rabbit muscle was examined with the electron microscope. In preparations of the completely converted glucose-6-phosphate dependent form (GSD) and the independent form (GSI) three structures were observed: toroids, hexagons and stacks of four elements which appear to be aggregates of four toroids.
Joseph Larner +2 more
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Regulation of hepatic glycogen phosphorylase and glycogen synthase by calcium and diacylglycerol
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1986Incubation of rat hepatocytes with angiotensin II (1 nM) produced a time-dependent accumulation of 1, 2-diacylglycerol and inactivation of glycogen synthase with maximum effects at 10 min. The level of diacylglycerol then gradually declined and the activity of glycogen synthase I returned to control values at 30 min.
John H. Exton, B Bouscarel
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An improved rapid assay of glycogen synthase
Analytical Biochemistry, 1979Abstract As an alternative to rapid filtration washing the glycogen free of any unreacted UDP-[14C]-glucose by ascending chromatography (ethanol:water, 2:1) can be used. This technique also makes the filter paper assay of glycogen synthase much faster: The samples are ready for liquid scintillation counting in 30 min.
Emma Villa-Moruzzi +2 more
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Indices of the activation state of glycogen synthase
Analytical Biochemistry, 1980Abstract Glucose 6-phosphate dependency relationships, Hill Plots, and apparent A0.5 glucose 6-phosphate values have been computed for mixtures of discrete forms of glycogen synthase. From these calculated values and by inspection of the ensuing graphs an asseessment can be made of the usefulness and limitations of I D relationships and A0.5 ...
Scott M. Van Patten, Donal A. Walsh
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Action pattern of muscle glycogen synthase
Molecular and Cellular Biochemistry, 1975The action pattern of muscle glycogen synthaseI form was investigated by means of a study of the distribution of radioactive glucosyl units in the glycogen synthesized under variable concentrations of the substrates UDP-glucose and glycogen. A multiple chain mechanism was found to be operative.
Eduardo Salsas, Joseph Larner
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Inhibition of Glycogen Synthase Kinase-3
2008There are two homologous forms of glycogen synthase kinase (GSK)-3, GSK-3alpha and GSK-3beta, which play overlapping roles in the regulation of Wnt, Hedgehog, and insulin pathways, as well as the activation of nuclear factor (NF)-kappaB-mediated gene transcription.
Daniel D. Billadeau, Andrei V. Ougolkov
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