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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| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_00032697_v147_n2_p491_Krisman |
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todo:paper_00032697_v147_n2_p491_Krisman2023-10-03T13:55:47Z Branching enzyme assay: Selective quantitation of the α1,6-linked glucosyl residues involved in the branching points Krisman, C.R. Tolmasky, D.S. Raffo, S. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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, C.R. Tolmasky, D.S. Raffo, S. 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. |
| format |
JOUR |
| author |
Krisman, C.R. Tolmasky, D.S. Raffo, S. |
| author_facet |
Krisman, C.R. Tolmasky, D.S. Raffo, S. |
| author_sort |
Krisman, C.R. |
| 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 |
| url |
http://hdl.handle.net/20.500.12110/paper_00032697_v147_n2_p491_Krisman |
| work_keys_str_mv |
AT krismancr branchingenzymeassayselectivequantitationofthea16linkedglucosylresiduesinvolvedinthebranchingpoints AT tolmaskyds branchingenzymeassayselectivequantitationofthea16linkedglucosylresiduesinvolvedinthebranchingpoints AT raffos branchingenzymeassayselectivequantitationofthea16linkedglucosylresiduesinvolvedinthebranchingpoints |
| _version_ |
1807324635758329856 |