In vitro synthesis of particulate glycogen from uridine diphosphate glucose. II. Some studies on the growth process

It was found that for the same extent of synthesis, the glycogen synthesized in vitro by liver glycogen synthetase (uridine diphosphate glucose: α-1,4-glucan α-4-glucosyltransferase, EC 2.4.1.11) from uridine diphosphate glucose is heavier than that synthesized from glucose 1-phosphate by muscle pho...

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Autores principales: Parodi, Armando José, Krisman de Fischman, Clara Rebeca
Publicado: 1970
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Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v141_n1_p219_Parodi
http://hdl.handle.net/20.500.12110/paper_00039861_v141_n1_p219_Parodi
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spelling paper:paper_00039861_v141_n1_p219_Parodi2023-06-08T14:24:55Z In vitro synthesis of particulate glycogen from uridine diphosphate glucose. II. Some studies on the growth process Parodi, Armando José Krisman de Fischman, Clara Rebeca glucosyltransferase glycogen hexose phosphate pyrimidine nucleotide animal article biosynthesis enzymology glycogen liver level kinetics liver metabolism molecular weight mouse muscle ultracentrifugation Animal Glucosyltransferases Glycogen Hexosephosphates Kinetics Liver Liver Glycogen Mice Molecular Weight Muscles Ultracentrifugation Uracil Nucleotides It was found that for the same extent of synthesis, the glycogen synthesized in vitro by liver glycogen synthetase (uridine diphosphate glucose: α-1,4-glucan α-4-glucosyltransferase, EC 2.4.1.11) from uridine diphosphate glucose is heavier than that synthesized from glucose 1-phosphate by muscle phosphorylase b (α-1,4 glucan:orthophosphate glucosyltransferase, EC 2.4.1.1). This result could be due to the different specificity of both transferring enzymes toward the molecular weight of the acceptor glycogen and to the incomplete use of the primer by glycogen synthetase. Glycogen synthesized from uridine diphosphate glucose showed a single light population in the first stages of synthesis. Later on, a clearly distinguishable heavier population appeared while the initial light peak was slightly shifted toward a higher molecular weight. The synthesis of glycogen from glucose 1-phosphate proceeded in a rather different way: only a single peak appeared during the synthesis. The molecular weight of this population increased as synthesis went on. An aggregation of the molecules of glycogen during synthesis from uridine diphosphate glucose could explain some of the results obtained. © 1970. Fil:Parodi, A.J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Krisman, C.R. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1970 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v141_n1_p219_Parodi http://hdl.handle.net/20.500.12110/paper_00039861_v141_n1_p219_Parodi
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic glucosyltransferase
glycogen
hexose phosphate
pyrimidine nucleotide
animal
article
biosynthesis
enzymology
glycogen liver level
kinetics
liver
metabolism
molecular weight
mouse
muscle
ultracentrifugation
Animal
Glucosyltransferases
Glycogen
Hexosephosphates
Kinetics
Liver
Liver Glycogen
Mice
Molecular Weight
Muscles
Ultracentrifugation
Uracil Nucleotides
spellingShingle glucosyltransferase
glycogen
hexose phosphate
pyrimidine nucleotide
animal
article
biosynthesis
enzymology
glycogen liver level
kinetics
liver
metabolism
molecular weight
mouse
muscle
ultracentrifugation
Animal
Glucosyltransferases
Glycogen
Hexosephosphates
Kinetics
Liver
Liver Glycogen
Mice
Molecular Weight
Muscles
Ultracentrifugation
Uracil Nucleotides
Parodi, Armando José
Krisman de Fischman, Clara Rebeca
In vitro synthesis of particulate glycogen from uridine diphosphate glucose. II. Some studies on the growth process
topic_facet glucosyltransferase
glycogen
hexose phosphate
pyrimidine nucleotide
animal
article
biosynthesis
enzymology
glycogen liver level
kinetics
liver
metabolism
molecular weight
mouse
muscle
ultracentrifugation
Animal
Glucosyltransferases
Glycogen
Hexosephosphates
Kinetics
Liver
Liver Glycogen
Mice
Molecular Weight
Muscles
Ultracentrifugation
Uracil Nucleotides
description It was found that for the same extent of synthesis, the glycogen synthesized in vitro by liver glycogen synthetase (uridine diphosphate glucose: α-1,4-glucan α-4-glucosyltransferase, EC 2.4.1.11) from uridine diphosphate glucose is heavier than that synthesized from glucose 1-phosphate by muscle phosphorylase b (α-1,4 glucan:orthophosphate glucosyltransferase, EC 2.4.1.1). This result could be due to the different specificity of both transferring enzymes toward the molecular weight of the acceptor glycogen and to the incomplete use of the primer by glycogen synthetase. Glycogen synthesized from uridine diphosphate glucose showed a single light population in the first stages of synthesis. Later on, a clearly distinguishable heavier population appeared while the initial light peak was slightly shifted toward a higher molecular weight. The synthesis of glycogen from glucose 1-phosphate proceeded in a rather different way: only a single peak appeared during the synthesis. The molecular weight of this population increased as synthesis went on. An aggregation of the molecules of glycogen during synthesis from uridine diphosphate glucose could explain some of the results obtained. © 1970.
author Parodi, Armando José
Krisman de Fischman, Clara Rebeca
author_facet Parodi, Armando José
Krisman de Fischman, Clara Rebeca
author_sort Parodi, Armando José
title In vitro synthesis of particulate glycogen from uridine diphosphate glucose. II. Some studies on the growth process
title_short In vitro synthesis of particulate glycogen from uridine diphosphate glucose. II. Some studies on the growth process
title_full In vitro synthesis of particulate glycogen from uridine diphosphate glucose. II. Some studies on the growth process
title_fullStr In vitro synthesis of particulate glycogen from uridine diphosphate glucose. II. Some studies on the growth process
title_full_unstemmed In vitro synthesis of particulate glycogen from uridine diphosphate glucose. II. Some studies on the growth process
title_sort in vitro synthesis of particulate glycogen from uridine diphosphate glucose. ii. some studies on the growth process
publishDate 1970
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v141_n1_p219_Parodi
http://hdl.handle.net/20.500.12110/paper_00039861_v141_n1_p219_Parodi
work_keys_str_mv AT parodiarmandojose invitrosynthesisofparticulateglycogenfromuridinediphosphateglucoseiisomestudiesonthegrowthprocess
AT krismandefischmanclararebeca invitrosynthesisofparticulateglycogenfromuridinediphosphateglucoseiisomestudiesonthegrowthprocess
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