A (1→4)-α-d-glucan-protein involved in liver glycogen biosynthesis
A macromolecular (1→4)-α-d-[14C]glucan-protein complex was synthesized with a rat liver preparation and uridine diphosphate d-[14C]glucose. The size of the complex is contributed by both the protein and the (1→4)-α-d-glucosyl-oligomer components. Iodoacetamide treatment did not change the migration...
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| Autores principales: | , |
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| Publicado: |
1986
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00086215_v149_n1_p35_Krisman http://hdl.handle.net/20.500.12110/paper_00086215_v149_n1_p35_Krisman |
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| Sumario: | A macromolecular (1→4)-α-d-[14C]glucan-protein complex was synthesized with a rat liver preparation and uridine diphosphate d-[14C]glucose. The size of the complex is contributed by both the protein and the (1→4)-α-d-glucosyl-oligomer components. Iodoacetamide treatment did not change the migration properties on Bio-Gel A-50m. Therefore, disulfide bonds linking glucan-protein subunits seem not to be involved. The [14C]glucan-protein, precipitated by diluted trichloroacetic acid, was digested by α-amylase, phosphorylase a, and proteases. The extent of proteolysis was greater for a complex having fewer d-glucose units incorporated. After proteolytic digestion of that complex, the labeled fragments behaved on electrophoresis, and ion-exchange and gel chromatography as [14C]glucosylated peptides. These findings support previous conclusions that the primer for liver glycogen synthesis is a protein on which glycogen is built up by covalent attachment. © 1986. |
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