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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todo:paper_00039861_v141_n1_p219_Parodi2023-10-03T13:56:50Z In vitro synthesis of particulate glycogen from uridine diphosphate glucose. II. Some studies on the growth process Parodi, A.J. Krisman, C.R. Mordoh, J. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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, A.J. Krisman, C.R. Mordoh, J. 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. |
| format |
JOUR |
| author |
Parodi, A.J. Krisman, C.R. Mordoh, J. |
| author_facet |
Parodi, A.J. Krisman, C.R. Mordoh, J. |
| author_sort |
Parodi, A.J. |
| 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 |
| url |
http://hdl.handle.net/20.500.12110/paper_00039861_v141_n1_p219_Parodi |
| work_keys_str_mv |
AT parodiaj invitrosynthesisofparticulateglycogenfromuridinediphosphateglucoseiisomestudiesonthegrowthprocess AT krismancr invitrosynthesisofparticulateglycogenfromuridinediphosphateglucoseiisomestudiesonthegrowthprocess AT mordohj invitrosynthesisofparticulateglycogenfromuridinediphosphateglucoseiisomestudiesonthegrowthprocess |
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1807323337066545152 |