Glycogen brain branching enzyme.

Rat brain glycogen branching enzyme was partially purified in order to elucidate its mechanism of action. The alpha1,4-alpha1,6-glucan polysaccharide was synthesized using rat brain branching enzyme under two different elongation conditions: Glc-1-P and phosphorylase or UDP-Glc and glycogen synthase...

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Autores principales: Tolmasky, Diana Silvia, Labriola, Carlos Alberto, Krisman de Fischman, Clara Rebeca
Publicado: 1998
Materias:
rat
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01455680_v44_n3_p455_Tolmasky
http://hdl.handle.net/20.500.12110/paper_01455680_v44_n3_p455_Tolmasky
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spelling paper:paper_01455680_v44_n3_p455_Tolmasky2023-06-08T15:12:23Z Glycogen brain branching enzyme. Tolmasky, Diana Silvia Labriola, Carlos Alberto Krisman de Fischman, Clara Rebeca 1,4 alpha glucan branching enzyme beta amylase glucose 1 phosphate glucose phosphate phosphorylase polysaccharide absorption animal article biosynthesis brain enzymology metabolism rat Wistar rat 1,4-alpha-Glucan Branching Enzyme Absorption Animals beta-Amylase Brain Glucosephosphates Phosphorylases Polysaccharides Rats Rats, Wistar Rat brain glycogen branching enzyme was partially purified in order to elucidate its mechanism of action. The alpha1,4-alpha1,6-glucan polysaccharide was synthesized using rat brain branching enzyme under two different elongation conditions: Glc-1-P and phosphorylase or UDP-Glc and glycogen synthase. The products obtained demonstrated that the cpolysaccharides synthesized (pattern of the spectra obtained in the presence of Krisman's reagent, lambda max, parameter A and R, % beta-amylolysis and degree of branching) under different incubation times are nearly constant. These results imply that the degree of branching of a polysaccharide depends only on the enzyme specificity. Fil:Tolmasky, D.S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Labriola, C. 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. 1998 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01455680_v44_n3_p455_Tolmasky http://hdl.handle.net/20.500.12110/paper_01455680_v44_n3_p455_Tolmasky
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic 1,4 alpha glucan branching enzyme
beta amylase
glucose 1 phosphate
glucose phosphate
phosphorylase
polysaccharide
absorption
animal
article
biosynthesis
brain
enzymology
metabolism
rat
Wistar rat
1,4-alpha-Glucan Branching Enzyme
Absorption
Animals
beta-Amylase
Brain
Glucosephosphates
Phosphorylases
Polysaccharides
Rats
Rats, Wistar
spellingShingle 1,4 alpha glucan branching enzyme
beta amylase
glucose 1 phosphate
glucose phosphate
phosphorylase
polysaccharide
absorption
animal
article
biosynthesis
brain
enzymology
metabolism
rat
Wistar rat
1,4-alpha-Glucan Branching Enzyme
Absorption
Animals
beta-Amylase
Brain
Glucosephosphates
Phosphorylases
Polysaccharides
Rats
Rats, Wistar
Tolmasky, Diana Silvia
Labriola, Carlos Alberto
Krisman de Fischman, Clara Rebeca
Glycogen brain branching enzyme.
topic_facet 1,4 alpha glucan branching enzyme
beta amylase
glucose 1 phosphate
glucose phosphate
phosphorylase
polysaccharide
absorption
animal
article
biosynthesis
brain
enzymology
metabolism
rat
Wistar rat
1,4-alpha-Glucan Branching Enzyme
Absorption
Animals
beta-Amylase
Brain
Glucosephosphates
Phosphorylases
Polysaccharides
Rats
Rats, Wistar
description Rat brain glycogen branching enzyme was partially purified in order to elucidate its mechanism of action. The alpha1,4-alpha1,6-glucan polysaccharide was synthesized using rat brain branching enzyme under two different elongation conditions: Glc-1-P and phosphorylase or UDP-Glc and glycogen synthase. The products obtained demonstrated that the cpolysaccharides synthesized (pattern of the spectra obtained in the presence of Krisman's reagent, lambda max, parameter A and R, % beta-amylolysis and degree of branching) under different incubation times are nearly constant. These results imply that the degree of branching of a polysaccharide depends only on the enzyme specificity.
author Tolmasky, Diana Silvia
Labriola, Carlos Alberto
Krisman de Fischman, Clara Rebeca
author_facet Tolmasky, Diana Silvia
Labriola, Carlos Alberto
Krisman de Fischman, Clara Rebeca
author_sort Tolmasky, Diana Silvia
title Glycogen brain branching enzyme.
title_short Glycogen brain branching enzyme.
title_full Glycogen brain branching enzyme.
title_fullStr Glycogen brain branching enzyme.
title_full_unstemmed Glycogen brain branching enzyme.
title_sort glycogen brain branching enzyme.
publishDate 1998
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01455680_v44_n3_p455_Tolmasky
http://hdl.handle.net/20.500.12110/paper_01455680_v44_n3_p455_Tolmasky
work_keys_str_mv AT tolmaskydianasilvia glycogenbrainbranchingenzyme
AT labriolacarlosalberto glycogenbrainbranchingenzyme
AT krismandefischmanclararebeca glycogenbrainbranchingenzyme
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