Results 111 to 120 of about 82,991 (164)
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Glycogen and glycogen synthase from pig leucocytes
International Journal of Biochemistry, 1979Abstract 1. 1. Pig polymorphonuclears and lymphocytes show a lower glycogen content than human leucocytes. 2. 2. The glycogen synthase activity from pig leucocytes has the same value as that from human leucocytes. 3. 3. Two forms of glycogen synthase interconvertible by phosphorylation-dephosphorylation reactions are present in pig ...
F, Pegueroles, R, Cussó
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Nuclear Glycogen and Glycogen Synthase Kinase 3
Biochemical and Biophysical Research Communications, 1998Glycogen is the principal storage form of glucose in animal cells. It accumulates in electron-dense cytoplasmic granules and is synthesized by glycogen synthase (GS), the rate-limiting enzyme of glycogen deposition. Glycogen synthase kinase-3 (GSK-3) is a protein kinase that phosphorylates GS.
M, Ragano-Caracciolo +3 more
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Localization of Glycogen Synthase in Brain
Journal of Neurochemistry, 1988AbstractAntisera against glycogen synthase from canine brain were prepared and used for investigation of the localization of the enzyme in the brain. Antisera cross‐reacted only with the 88‐kilodalton protein that is the subunit of brain glycogen synthase.
N, Inoue +3 more
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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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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 D, Newman, J M, Armstrong
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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.
M 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.
M G, Hegazy +3 more
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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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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
M C, Gannon, F Q, Nuttall
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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
M C, Gannon, F Q, Nuttall
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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.
B, Bouscarel, J H, Exton
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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.
A, Akatsuka, T J, Singh, K P, Huang
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