The degree of branching in (α1,4)‐(α1,6)‐linked glucopolysaccharides is dependent on intrinsic properties of the branching enzymes
Branching enzymes from rat and rabbit liver, as well as from potato and maize were prepared. They were almost free from contaminating glucan‐degrading enzymes. In ‘sweet corn’ maize, two separate fractions with (α1,4)glucan: (α1,4)glucan α6‐glycosyltransferase activities were obtained. One of them s...
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todo:paper_00142956_v168_n2_p393_Tolmasky2023-10-03T14:11:50Z The degree of branching in (α1,4)‐(α1,6)‐linked glucopolysaccharides is dependent on intrinsic properties of the branching enzymes Tolmasky, D.S. Krisman, C.R. 1,4 alpha glucan branching enzyme amylopectin elongation factor glucosyltransferase glycogen synthase phosphorylase polysaccharide animal article atomic absorption spectrometry biosynthesis enzymology glycogen liver level in vitro study liver maize metabolism potato rabbit rat structure activity relation 1,4-alpha-Glucan Branching Enzyme Amylopectin Animal Glucosyltransferases Glycogen Synthase In Vitro Liver Liver Glycogen Peptide Elongation Factors Phosphorylases Polysaccharides Potatoes Rabbits Rats Spectrophotometry, Atomic Absorption Structure-Activity Relationship Support, Non-U.S. Gov't Zea mays Branching enzymes from rat and rabbit liver, as well as from potato and maize were prepared. They were almost free from contaminating glucan‐degrading enzymes. In ‘sweet corn’ maize, two separate fractions with (α1,4)glucan: (α1,4)glucan α6‐glycosyltransferase activities were obtained. One of them synthesized amylopectin, the branched component of starch, in the presence of phosphorylase and Glc1P, while the other fraction synthesized phytoglycogen. Furthermore, in a maize variety which does not accumulate phytoglycogen, only one fraction of branching activity was found, that formed amylopectin under the above‐mentioned conditions. Comparative analyses performed with native (α1,4)‐(α1,6)glucopolysaccharides, and those synthesized in vitro with the branching enzyme from the same tissue, demonstrated a close similarity between both glucans. It may be concluded that the branching enzyme is responsible for the specific degree of (α1,6) branch linkages found in the native polysaccharide. Copyright © 1987, Wiley Blackwell. All rights reserved Fil:Tolmasky, D.S. 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_00142956_v168_n2_p393_Tolmasky |
| institution |
Universidad de Buenos Aires |
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I-28 |
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R-134 |
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
1,4 alpha glucan branching enzyme amylopectin elongation factor glucosyltransferase glycogen synthase phosphorylase polysaccharide animal article atomic absorption spectrometry biosynthesis enzymology glycogen liver level in vitro study liver maize metabolism potato rabbit rat structure activity relation 1,4-alpha-Glucan Branching Enzyme Amylopectin Animal Glucosyltransferases Glycogen Synthase In Vitro Liver Liver Glycogen Peptide Elongation Factors Phosphorylases Polysaccharides Potatoes Rabbits Rats Spectrophotometry, Atomic Absorption Structure-Activity Relationship Support, Non-U.S. Gov't Zea mays |
| spellingShingle |
1,4 alpha glucan branching enzyme amylopectin elongation factor glucosyltransferase glycogen synthase phosphorylase polysaccharide animal article atomic absorption spectrometry biosynthesis enzymology glycogen liver level in vitro study liver maize metabolism potato rabbit rat structure activity relation 1,4-alpha-Glucan Branching Enzyme Amylopectin Animal Glucosyltransferases Glycogen Synthase In Vitro Liver Liver Glycogen Peptide Elongation Factors Phosphorylases Polysaccharides Potatoes Rabbits Rats Spectrophotometry, Atomic Absorption Structure-Activity Relationship Support, Non-U.S. Gov't Zea mays Tolmasky, D.S. Krisman, C.R. The degree of branching in (α1,4)‐(α1,6)‐linked glucopolysaccharides is dependent on intrinsic properties of the branching enzymes |
| topic_facet |
1,4 alpha glucan branching enzyme amylopectin elongation factor glucosyltransferase glycogen synthase phosphorylase polysaccharide animal article atomic absorption spectrometry biosynthesis enzymology glycogen liver level in vitro study liver maize metabolism potato rabbit rat structure activity relation 1,4-alpha-Glucan Branching Enzyme Amylopectin Animal Glucosyltransferases Glycogen Synthase In Vitro Liver Liver Glycogen Peptide Elongation Factors Phosphorylases Polysaccharides Potatoes Rabbits Rats Spectrophotometry, Atomic Absorption Structure-Activity Relationship Support, Non-U.S. Gov't Zea mays |
| description |
Branching enzymes from rat and rabbit liver, as well as from potato and maize were prepared. They were almost free from contaminating glucan‐degrading enzymes. In ‘sweet corn’ maize, two separate fractions with (α1,4)glucan: (α1,4)glucan α6‐glycosyltransferase activities were obtained. One of them synthesized amylopectin, the branched component of starch, in the presence of phosphorylase and Glc1P, while the other fraction synthesized phytoglycogen. Furthermore, in a maize variety which does not accumulate phytoglycogen, only one fraction of branching activity was found, that formed amylopectin under the above‐mentioned conditions. Comparative analyses performed with native (α1,4)‐(α1,6)glucopolysaccharides, and those synthesized in vitro with the branching enzyme from the same tissue, demonstrated a close similarity between both glucans. It may be concluded that the branching enzyme is responsible for the specific degree of (α1,6) branch linkages found in the native polysaccharide. Copyright © 1987, Wiley Blackwell. All rights reserved |
| format |
JOUR |
| author |
Tolmasky, D.S. Krisman, C.R. |
| author_facet |
Tolmasky, D.S. Krisman, C.R. |
| author_sort |
Tolmasky, D.S. |
| title |
The degree of branching in (α1,4)‐(α1,6)‐linked glucopolysaccharides is dependent on intrinsic properties of the branching enzymes |
| title_short |
The degree of branching in (α1,4)‐(α1,6)‐linked glucopolysaccharides is dependent on intrinsic properties of the branching enzymes |
| title_full |
The degree of branching in (α1,4)‐(α1,6)‐linked glucopolysaccharides is dependent on intrinsic properties of the branching enzymes |
| title_fullStr |
The degree of branching in (α1,4)‐(α1,6)‐linked glucopolysaccharides is dependent on intrinsic properties of the branching enzymes |
| title_full_unstemmed |
The degree of branching in (α1,4)‐(α1,6)‐linked glucopolysaccharides is dependent on intrinsic properties of the branching enzymes |
| title_sort |
degree of branching in (α1,4)‐(α1,6)‐linked glucopolysaccharides is dependent on intrinsic properties of the branching enzymes |
| url |
http://hdl.handle.net/20.500.12110/paper_00142956_v168_n2_p393_Tolmasky |
| work_keys_str_mv |
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