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: Krisman de Fischman, Clara Rebeca, Geremía, Roberto Alejandro
Publicado: 1986
Materias:
rat
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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spelling paper:paper_00086215_v149_n1_p35_Krisman2023-06-08T14:32:15Z A (1→4)-α-d-glucan-protein involved in liver glycogen biosynthesis Krisman de Fischman, Clara Rebeca Geremía, Roberto Alejandro carbon glucan glycoprotein uridine diphosphate glucose animal article biosynthesis enzymology gel chromatography glycogen liver level ion exchange chromatography liver metabolism paper electrophoresis rat Animal Carbon Radioisotopes Chromatography, Gel Chromatography, Ion Exchange Electrophoresis, Paper Glucans Glycoproteins Liver Liver Glycogen Rats Support, Non-U.S. Gov't Support, U.S. Gov't, P.H.S. Uridine Diphosphate Glucose 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. Fil:Krisman, C.R. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Geremia, R.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1986 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
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic carbon
glucan
glycoprotein
uridine diphosphate glucose
animal
article
biosynthesis
enzymology
gel chromatography
glycogen liver level
ion exchange chromatography
liver
metabolism
paper electrophoresis
rat
Animal
Carbon Radioisotopes
Chromatography, Gel
Chromatography, Ion Exchange
Electrophoresis, Paper
Glucans
Glycoproteins
Liver
Liver Glycogen
Rats
Support, Non-U.S. Gov't
Support, U.S. Gov't, P.H.S.
Uridine Diphosphate Glucose
spellingShingle carbon
glucan
glycoprotein
uridine diphosphate glucose
animal
article
biosynthesis
enzymology
gel chromatography
glycogen liver level
ion exchange chromatography
liver
metabolism
paper electrophoresis
rat
Animal
Carbon Radioisotopes
Chromatography, Gel
Chromatography, Ion Exchange
Electrophoresis, Paper
Glucans
Glycoproteins
Liver
Liver Glycogen
Rats
Support, Non-U.S. Gov't
Support, U.S. Gov't, P.H.S.
Uridine Diphosphate Glucose
Krisman de Fischman, Clara Rebeca
Geremía, Roberto Alejandro
A (1→4)-α-d-glucan-protein involved in liver glycogen biosynthesis
topic_facet carbon
glucan
glycoprotein
uridine diphosphate glucose
animal
article
biosynthesis
enzymology
gel chromatography
glycogen liver level
ion exchange chromatography
liver
metabolism
paper electrophoresis
rat
Animal
Carbon Radioisotopes
Chromatography, Gel
Chromatography, Ion Exchange
Electrophoresis, Paper
Glucans
Glycoproteins
Liver
Liver Glycogen
Rats
Support, Non-U.S. Gov't
Support, U.S. Gov't, P.H.S.
Uridine Diphosphate Glucose
description 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.
author Krisman de Fischman, Clara Rebeca
Geremía, Roberto Alejandro
author_facet Krisman de Fischman, Clara Rebeca
Geremía, Roberto Alejandro
author_sort Krisman de Fischman, Clara Rebeca
title A (1→4)-α-d-glucan-protein involved in liver glycogen biosynthesis
title_short A (1→4)-α-d-glucan-protein involved in liver glycogen biosynthesis
title_full A (1→4)-α-d-glucan-protein involved in liver glycogen biosynthesis
title_fullStr A (1→4)-α-d-glucan-protein involved in liver glycogen biosynthesis
title_full_unstemmed A (1→4)-α-d-glucan-protein involved in liver glycogen biosynthesis
title_sort (1→4)-α-d-glucan-protein involved in liver glycogen biosynthesis
publishDate 1986
url 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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