Results 301 to 310 of about 454,859 (358)
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Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1989
Several polycations were tested for their abilities to inhibit the activity of glycogen synthase kinase 3 (GSK-3). L-Polylysine was the most powerful inhibitor of GSK-3 with half-maximal inhibition of glycogen synthase phosphorylation occurring at approx. 100 nM.
Mohammed G. Hegazy +3 more
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Several polycations were tested for their abilities to inhibit the activity of glycogen synthase kinase 3 (GSK-3). L-Polylysine was the most powerful inhibitor of GSK-3 with half-maximal inhibition of glycogen synthase phosphorylation occurring at approx. 100 nM.
Mohammed G. Hegazy +3 more
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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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Diabetes, 1972
The present status of the molecular nature of the enzyme glycogen synthase from rabbit skeletal muscle is reviewed. It is shown that per 90,000 Dalton subunit there are six phosphorylatable sites and six sulfhydryl groups. No pyridoxal phosphate is present.
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The present status of the molecular nature of the enzyme glycogen synthase from rabbit skeletal muscle is reviewed. It is shown that per 90,000 Dalton subunit there are six phosphorylatable sites and six sulfhydryl groups. No pyridoxal phosphate is present.
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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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Purification of bovine heart glycogen synthase
Analytical Biochemistry, 1985Glycogen synthase was purified to apparent homogeneity from bovine heart muscle by a procedure involving precipitation of the enzyme in the presence of added glycogen by polyethylene glycol, chromatography on DEAE-Sephacel, and high-speed centrifugation through a sucrose-containing buffer.
Dickey-Dunkirk S, Killilea Sd
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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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