The initiation of glycogen biosynthesis in rat heart α‐1,4 glucans tightly associated with glycogen synthase
A partially purified glycogen synthase from rat cardiac muscle transferred glucosyl residues from UDP‐[14C]glucose to an endogenous protein acceptor in the absence of added primer. After native gel electrophoresis of the enzyme preparation, unprimed activity was detected. Primer‐dependent and indepe...
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todo:paper_00142956_v156_n1_p163_BLUMENFELD2023-10-03T14:11:49Z The initiation of glycogen biosynthesis in rat heart α‐1,4 glucans tightly associated with glycogen synthase BLUMENFELD, M.L. KRISMAN, C.R. glycogen glycogen synthase alpha 1,4 glucan animal cell biosynthesis heart nonhuman priority journal rat alpha-Amylase Animal Binding Sites Electrophoresis, Polyacrylamide Gel Glucans Glucose Glycogen Glycogen Synthase Myocardium Protein Binding Rats Solubility Support, Non-U.S. Gov't A partially purified glycogen synthase from rat cardiac muscle transferred glucosyl residues from UDP‐[14C]glucose to an endogenous protein acceptor in the absence of added primer. After native gel electrophoresis of the enzyme preparation, unprimed activity was detected. Primer‐dependent and independent activities were found in the same position. After denaturing gel electrophoresis of the reaction products, radioactivity comigrated with protein. Pulse‐chase experiments showed that the size of the reaction products increased as a function of time. These products were degraded by amyloglucosidase, thus suggesting that glycogen‐like molecules had grown on the protein acceptor. The activity of the enzyme was markedly reduced upon preincubation with α‐amylase. Therefore, preformed protein‐bound α‐1,4‐glucans were acting as primers. The glucoprotein acceptor may be a protein strongly associated with glycogen synthease, or alternatively, the enzyme itself. Copyright © 1986, Wiley Blackwell. All rights reserved Fil:BLUMENFELD, M.L. 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_00142956_v156_n1_p163_BLUMENFELD |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
glycogen glycogen synthase alpha 1,4 glucan animal cell biosynthesis heart nonhuman priority journal rat alpha-Amylase Animal Binding Sites Electrophoresis, Polyacrylamide Gel Glucans Glucose Glycogen Glycogen Synthase Myocardium Protein Binding Rats Solubility Support, Non-U.S. Gov't |
| spellingShingle |
glycogen glycogen synthase alpha 1,4 glucan animal cell biosynthesis heart nonhuman priority journal rat alpha-Amylase Animal Binding Sites Electrophoresis, Polyacrylamide Gel Glucans Glucose Glycogen Glycogen Synthase Myocardium Protein Binding Rats Solubility Support, Non-U.S. Gov't BLUMENFELD, M.L. KRISMAN, C.R. The initiation of glycogen biosynthesis in rat heart α‐1,4 glucans tightly associated with glycogen synthase |
| topic_facet |
glycogen glycogen synthase alpha 1,4 glucan animal cell biosynthesis heart nonhuman priority journal rat alpha-Amylase Animal Binding Sites Electrophoresis, Polyacrylamide Gel Glucans Glucose Glycogen Glycogen Synthase Myocardium Protein Binding Rats Solubility Support, Non-U.S. Gov't |
| description |
A partially purified glycogen synthase from rat cardiac muscle transferred glucosyl residues from UDP‐[14C]glucose to an endogenous protein acceptor in the absence of added primer. After native gel electrophoresis of the enzyme preparation, unprimed activity was detected. Primer‐dependent and independent activities were found in the same position. After denaturing gel electrophoresis of the reaction products, radioactivity comigrated with protein. Pulse‐chase experiments showed that the size of the reaction products increased as a function of time. These products were degraded by amyloglucosidase, thus suggesting that glycogen‐like molecules had grown on the protein acceptor. The activity of the enzyme was markedly reduced upon preincubation with α‐amylase. Therefore, preformed protein‐bound α‐1,4‐glucans were acting as primers. The glucoprotein acceptor may be a protein strongly associated with glycogen synthease, or alternatively, the enzyme itself. Copyright © 1986, Wiley Blackwell. All rights reserved |
| format |
JOUR |
| author |
BLUMENFELD, M.L. KRISMAN, C.R. |
| author_facet |
BLUMENFELD, M.L. KRISMAN, C.R. |
| author_sort |
BLUMENFELD, M.L. |
| title |
The initiation of glycogen biosynthesis in rat heart α‐1,4 glucans tightly associated with glycogen synthase |
| title_short |
The initiation of glycogen biosynthesis in rat heart α‐1,4 glucans tightly associated with glycogen synthase |
| title_full |
The initiation of glycogen biosynthesis in rat heart α‐1,4 glucans tightly associated with glycogen synthase |
| title_fullStr |
The initiation of glycogen biosynthesis in rat heart α‐1,4 glucans tightly associated with glycogen synthase |
| title_full_unstemmed |
The initiation of glycogen biosynthesis in rat heart α‐1,4 glucans tightly associated with glycogen synthase |
| title_sort |
initiation of glycogen biosynthesis in rat heart α‐1,4 glucans tightly associated with glycogen synthase |
| url |
http://hdl.handle.net/20.500.12110/paper_00142956_v156_n1_p163_BLUMENFELD |
| work_keys_str_mv |
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1782031115776688128 |