Branching enzyme assay: Selective quantitation of the α1,6-linked glucosyl residues involved in the branching points

Methods previously described for glycogen or amylopectin branching enzymatic activity are insufficiently sensitive and not quantitative. A new, more sensitive, specific, and quantitative one was developed. It is based upon the quantitation of the glucose residues joined by α1,6 bonds introduced by v...

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Autores principales: Krisman de Fischman, Clara Rebeca, Tolmasky, Diana Silvia
Publicado: 1985
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Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00032697_v147_n2_p491_Krisman
http://hdl.handle.net/20.500.12110/paper_00032697_v147_n2_p491_Krisman
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spelling paper:paper_00032697_v147_n2_p491_Krisman2023-06-08T14:23:59Z Branching enzyme assay: Selective quantitation of the α1,6-linked glucosyl residues involved in the branching points Krisman de Fischman, Clara Rebeca Tolmasky, Diana Silvia amylo-α1,4-α1,6-transglucosylase amylopectin branching enzyme assay glycogen quantitation of branching points α1,6-glucosydic linkage 1,4 alpha glucan branching enzyme enzyme assay nonhuman priority journal 1,4-alpha-Glucan Branching Enzyme Animal Glucans Glucosyltransferases Polysaccharides Rabbits Methods previously described for glycogen or amylopectin branching enzymatic activity are insufficiently sensitive and not quantitative. A new, more sensitive, specific, and quantitative one was developed. It is based upon the quantitation of the glucose residues joined by α1,6 bonds introduced by varying amounts of branching enzyme. The procedure involved the synthesis of a polysaccharide from Glc-1-P and phosphorylase in the presence of the sample to be tested. The branched polysaccharide was then purified and the glucoses involved in the branching points were quantitated after degradation with phosphorylase and debranching enzymes. This method appeared to be useful, not only in enzymatic activity determinations but also in the study of the structure of α-d-glucans when combined with those of total polysaccharide quantitation, such as iodine and phenol-sulfuric acid. © 1985. Fil:Krisman, C.R. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Tolmasky, D.S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1985 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00032697_v147_n2_p491_Krisman http://hdl.handle.net/20.500.12110/paper_00032697_v147_n2_p491_Krisman
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic amylo-α1,4-α1,6-transglucosylase
amylopectin
branching enzyme assay
glycogen
quantitation of branching points
α1,6-glucosydic linkage
1,4 alpha glucan branching enzyme
enzyme assay
nonhuman
priority journal
1,4-alpha-Glucan Branching Enzyme
Animal
Glucans
Glucosyltransferases
Polysaccharides
Rabbits
spellingShingle amylo-α1,4-α1,6-transglucosylase
amylopectin
branching enzyme assay
glycogen
quantitation of branching points
α1,6-glucosydic linkage
1,4 alpha glucan branching enzyme
enzyme assay
nonhuman
priority journal
1,4-alpha-Glucan Branching Enzyme
Animal
Glucans
Glucosyltransferases
Polysaccharides
Rabbits
Krisman de Fischman, Clara Rebeca
Tolmasky, Diana Silvia
Branching enzyme assay: Selective quantitation of the α1,6-linked glucosyl residues involved in the branching points
topic_facet amylo-α1,4-α1,6-transglucosylase
amylopectin
branching enzyme assay
glycogen
quantitation of branching points
α1,6-glucosydic linkage
1,4 alpha glucan branching enzyme
enzyme assay
nonhuman
priority journal
1,4-alpha-Glucan Branching Enzyme
Animal
Glucans
Glucosyltransferases
Polysaccharides
Rabbits
description Methods previously described for glycogen or amylopectin branching enzymatic activity are insufficiently sensitive and not quantitative. A new, more sensitive, specific, and quantitative one was developed. It is based upon the quantitation of the glucose residues joined by α1,6 bonds introduced by varying amounts of branching enzyme. The procedure involved the synthesis of a polysaccharide from Glc-1-P and phosphorylase in the presence of the sample to be tested. The branched polysaccharide was then purified and the glucoses involved in the branching points were quantitated after degradation with phosphorylase and debranching enzymes. This method appeared to be useful, not only in enzymatic activity determinations but also in the study of the structure of α-d-glucans when combined with those of total polysaccharide quantitation, such as iodine and phenol-sulfuric acid. © 1985.
author Krisman de Fischman, Clara Rebeca
Tolmasky, Diana Silvia
author_facet Krisman de Fischman, Clara Rebeca
Tolmasky, Diana Silvia
author_sort Krisman de Fischman, Clara Rebeca
title Branching enzyme assay: Selective quantitation of the α1,6-linked glucosyl residues involved in the branching points
title_short Branching enzyme assay: Selective quantitation of the α1,6-linked glucosyl residues involved in the branching points
title_full Branching enzyme assay: Selective quantitation of the α1,6-linked glucosyl residues involved in the branching points
title_fullStr Branching enzyme assay: Selective quantitation of the α1,6-linked glucosyl residues involved in the branching points
title_full_unstemmed Branching enzyme assay: Selective quantitation of the α1,6-linked glucosyl residues involved in the branching points
title_sort branching enzyme assay: selective quantitation of the α1,6-linked glucosyl residues involved in the branching points
publishDate 1985
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00032697_v147_n2_p491_Krisman
http://hdl.handle.net/20.500.12110/paper_00032697_v147_n2_p491_Krisman
work_keys_str_mv AT krismandefischmanclararebeca branchingenzymeassayselectivequantitationofthea16linkedglucosylresiduesinvolvedinthebranchingpoints
AT tolmaskydianasilvia branchingenzymeassayselectivequantitationofthea16linkedglucosylresiduesinvolvedinthebranchingpoints
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