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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todo:paper_00086215_v149_n1_p35_Krisman2023-10-03T14:06:21Z A (1→4)-α-d-glucan-protein involved in liver glycogen biosynthesis Krisman, C.R. Geremia, R.A. Whelan, W.J. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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, C.R. Geremia, R.A. Whelan, W.J. 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. |
| format |
JOUR |
| author |
Krisman, C.R. Geremia, R.A. Whelan, W.J. |
| author_facet |
Krisman, C.R. Geremia, R.A. Whelan, W.J. |
| author_sort |
Krisman, C.R. |
| 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 |
| url |
http://hdl.handle.net/20.500.12110/paper_00086215_v149_n1_p35_Krisman |
| work_keys_str_mv |
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