Biosynthesis of glycogen from uridine diphosphate glucose

An enzyme which leads to the formation of glycogen according to the equation: UDPG + primer → UDP + glucosyl α (1 → 4) primer has been studied. The optimal conditions for activity were determined with a partially purified preparation from rat muscle. The reaction requires the presence of a polysacch...

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Detalles Bibliográficos
Autores principales:	Goldemberg, Sara Hebe, Carminatti, Héctor
Publicado:	1959
Materias:	glycogen nucleoside nucleotide article GLYCOGEN/metabolism metabolism muscle MUSCLES/metabolism NUCLEOSIDES AND NUCLEOTIDES/metabolism Glycogen Muscles Nucleosides Nucleotides
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v81_n2_p508_Leloir http://hdl.handle.net/20.500.12110/paper_00039861_v81_n2_p508_Leloir
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_00039861_v81_n2_p508_Leloir
record_format	dspace
spelling	paper:paper_00039861_v81_n2_p508_Leloir2023-06-08T14:25:07Z Biosynthesis of glycogen from uridine diphosphate glucose Goldemberg, Sara Hebe Carminatti, Héctor glycogen nucleoside nucleotide article GLYCOGEN/metabolism metabolism muscle MUSCLES/metabolism NUCLEOSIDES AND NUCLEOTIDES/metabolism GLYCOGEN/metabolism MUSCLES/metabolism NUCLEOSIDES AND NUCLEOTIDES/metabolism Glycogen Muscles Nucleosides Nucleotides An enzyme which leads to the formation of glycogen according to the equation: UDPG + primer → UDP + glucosyl α (1 → 4) primer has been studied. The optimal conditions for activity were determined with a partially purified preparation from rat muscle. The reaction requires the presence of a polysaccharide as primer and is strongly activated by hexose 6-phosphates. Using UDPG labeled in the glucose moiety, it was found that the radioactivity was transferred to the glycogen from which it could be removed as maltose with β-amylase or as G-1-P with phosphorylase. Thus it seems that the glucose residue becomes linked α (1 → 4) to the polysaccharide. Several inhibitors were tested as well as the occurrence of the enzyme in different organs. © 1959. Fil:Goldemberg, S.H. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Carminatti, H. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1959 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v81_n2_p508_Leloir http://hdl.handle.net/20.500.12110/paper_00039861_v81_n2_p508_Leloir
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 nucleoside nucleotide article GLYCOGEN/metabolism metabolism muscle MUSCLES/metabolism NUCLEOSIDES AND NUCLEOTIDES/metabolism GLYCOGEN/metabolism MUSCLES/metabolism NUCLEOSIDES AND NUCLEOTIDES/metabolism Glycogen Muscles Nucleosides Nucleotides
spellingShingle	glycogen nucleoside nucleotide article GLYCOGEN/metabolism metabolism muscle MUSCLES/metabolism NUCLEOSIDES AND NUCLEOTIDES/metabolism GLYCOGEN/metabolism MUSCLES/metabolism NUCLEOSIDES AND NUCLEOTIDES/metabolism Glycogen Muscles Nucleosides Nucleotides Goldemberg, Sara Hebe Carminatti, Héctor Biosynthesis of glycogen from uridine diphosphate glucose
topic_facet	glycogen nucleoside nucleotide article GLYCOGEN/metabolism metabolism muscle MUSCLES/metabolism NUCLEOSIDES AND NUCLEOTIDES/metabolism GLYCOGEN/metabolism MUSCLES/metabolism NUCLEOSIDES AND NUCLEOTIDES/metabolism Glycogen Muscles Nucleosides Nucleotides
description	An enzyme which leads to the formation of glycogen according to the equation: UDPG + primer → UDP + glucosyl α (1 → 4) primer has been studied. The optimal conditions for activity were determined with a partially purified preparation from rat muscle. The reaction requires the presence of a polysaccharide as primer and is strongly activated by hexose 6-phosphates. Using UDPG labeled in the glucose moiety, it was found that the radioactivity was transferred to the glycogen from which it could be removed as maltose with β-amylase or as G-1-P with phosphorylase. Thus it seems that the glucose residue becomes linked α (1 → 4) to the polysaccharide. Several inhibitors were tested as well as the occurrence of the enzyme in different organs. © 1959.
author	Goldemberg, Sara Hebe Carminatti, Héctor
author_facet	Goldemberg, Sara Hebe Carminatti, Héctor
author_sort	Goldemberg, Sara Hebe
title	Biosynthesis of glycogen from uridine diphosphate glucose
title_short	Biosynthesis of glycogen from uridine diphosphate glucose
title_full	Biosynthesis of glycogen from uridine diphosphate glucose
title_fullStr	Biosynthesis of glycogen from uridine diphosphate glucose
title_full_unstemmed	Biosynthesis of glycogen from uridine diphosphate glucose
title_sort	biosynthesis of glycogen from uridine diphosphate glucose
publishDate	1959
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v81_n2_p508_Leloir http://hdl.handle.net/20.500.12110/paper_00039861_v81_n2_p508_Leloir
work_keys_str_mv	AT goldembergsarahebe biosynthesisofglycogenfromuridinediphosphateglucose AT carminattihector biosynthesisofglycogenfromuridinediphosphateglucose
_version_	1768544938313646080

Biosynthesis of glycogen from uridine diphosphate glucose

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