Results 201 to 210 of about 147,796 (254)
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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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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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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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[Glycogen synthase gene-glycogen synthase gene in Japanese patients with NIDDM].
Nihon rinsho. Japanese journal of clinical medicine, 1995As glycogen synthase is a key enzyme of the non-oxidative pathway of glucose metabolism in the skeletal muscle, and reduced activity of this enzyme is related to insulin resistance, it seems likely that this enzyme is a candidate gene for contributing to the pathogenesis of NIDDM.
H, Kuroyama, T, Sanke, K, Nanjo
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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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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.
L I, Rebhun, C, Smith, J, Larner
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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.
S, Dickey-Dunkirk, S D, Killilea
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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.
E, Salsas, J, Larner
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Thyroid Hormones Regulate Hepatic Glycogen Synthase*
Endocrinology, 1984Short term (48 h) in vivo administration of either T3 or T4 was associated with an increase in hepatic glycogen synthase activity in the rat. Administration of 0.25 mg T3/kg BW 48, 24, and 2 h before enzyme preparation increased the total glycogen synthase activity by approximately 50% and increased the percentage of synthase in the I or active form ...
C C, Malbon, R, Campbell
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1986
Publisher Summary This chapter reviews knowledge of mammalian liver glycogen synthase and its short-term regulation by covalent phosphorylation mechanisms. Elevated concentrations of insulin and glucose promote glycogen synthesis and the activation of glycogen synthase.
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Publisher Summary This chapter reviews knowledge of mammalian liver glycogen synthase and its short-term regulation by covalent phosphorylation mechanisms. Elevated concentrations of insulin and glucose promote glycogen synthesis and the activation of glycogen synthase.
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