α‐Glucan synthesis on a protein primer: A reconstituted system for the formation of protein‐bound α‐glucan

Reconstitution experiments with the DEAE‐cellulose‐treated enzymes, engaged in a two‐step mechanism of synthesis of α‐glucan bound to protein, are performed. Urea/sodium dodecyl sulfate/polyacrylamide gel electrophoretic analysis of the radioactive products synthesized by the reconstituted system sh...

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Autores principales: MORENO, S., CARDINI, C.E., TANDECARZ, J.S.
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Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00142956_v162_n3_p609_MORENO
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spelling todo:paper_00142956_v162_n3_p609_MORENO2023-10-03T14:11:50Z α‐Glucan synthesis on a protein primer: A reconstituted system for the formation of protein‐bound α‐glucan MORENO, S. CARDINI, C.E. TANDECARZ, J.S. 1,4 glucan 1,4-glucan beta amylase glucan phosphorylase starch synthase vegetable protein article biosynthesis catalysis fluorography metabolism polyacrylamide gel electrophoresis potato protein binding beta-Amylase Catalysis Electrophoresis, Polyacrylamide Gel Glucans Phosphorylases Photofluorography Plant Proteins Potatoes Protein Binding Starch Synthase Support, Non-U.S. Gov't Reconstitution experiments with the DEAE‐cellulose‐treated enzymes, engaged in a two‐step mechanism of synthesis of α‐glucan bound to protein, are performed. Urea/sodium dodecyl sulfate/polyacrylamide gel electrophoretic analysis of the radioactive products synthesized by the reconstituted system shows highly glucosylated, labeled bands, whose apparent molecular masses change with the acrylamide concentration in the gels. The long carbohydrate chains synthesized during the second step arise from the sequential addition of glucosyl moieties to the glucoprotein formed during the first step. A deglucosylation experiment confirms that the product of the reconstituted system originates from the 38‐kDa glucosylated component of the reaction 1 product by the addition of β‐amylase‐sensitive glucosyl moieties. Our data suggest that specific phosphorylases and starch synthetases are found in potato tuber, which are capable of utilizing reaction 1 product as primer for the synthesis of protein‐bound glucan. Copyright © 1987, Wiley Blackwell. All rights reserved Fil:MORENO, S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:TANDECARZ, J.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_00142956_v162_n3_p609_MORENO
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 glucan
1,4-glucan
beta amylase
glucan
phosphorylase
starch synthase
vegetable protein
article
biosynthesis
catalysis
fluorography
metabolism
polyacrylamide gel electrophoresis
potato
protein binding
beta-Amylase
Catalysis
Electrophoresis, Polyacrylamide Gel
Glucans
Phosphorylases
Photofluorography
Plant Proteins
Potatoes
Protein Binding
Starch Synthase
Support, Non-U.S. Gov't
spellingShingle 1,4 glucan
1,4-glucan
beta amylase
glucan
phosphorylase
starch synthase
vegetable protein
article
biosynthesis
catalysis
fluorography
metabolism
polyacrylamide gel electrophoresis
potato
protein binding
beta-Amylase
Catalysis
Electrophoresis, Polyacrylamide Gel
Glucans
Phosphorylases
Photofluorography
Plant Proteins
Potatoes
Protein Binding
Starch Synthase
Support, Non-U.S. Gov't
MORENO, S.
CARDINI, C.E.
TANDECARZ, J.S.
α‐Glucan synthesis on a protein primer: A reconstituted system for the formation of protein‐bound α‐glucan
topic_facet 1,4 glucan
1,4-glucan
beta amylase
glucan
phosphorylase
starch synthase
vegetable protein
article
biosynthesis
catalysis
fluorography
metabolism
polyacrylamide gel electrophoresis
potato
protein binding
beta-Amylase
Catalysis
Electrophoresis, Polyacrylamide Gel
Glucans
Phosphorylases
Photofluorography
Plant Proteins
Potatoes
Protein Binding
Starch Synthase
Support, Non-U.S. Gov't
description Reconstitution experiments with the DEAE‐cellulose‐treated enzymes, engaged in a two‐step mechanism of synthesis of α‐glucan bound to protein, are performed. Urea/sodium dodecyl sulfate/polyacrylamide gel electrophoretic analysis of the radioactive products synthesized by the reconstituted system shows highly glucosylated, labeled bands, whose apparent molecular masses change with the acrylamide concentration in the gels. The long carbohydrate chains synthesized during the second step arise from the sequential addition of glucosyl moieties to the glucoprotein formed during the first step. A deglucosylation experiment confirms that the product of the reconstituted system originates from the 38‐kDa glucosylated component of the reaction 1 product by the addition of β‐amylase‐sensitive glucosyl moieties. Our data suggest that specific phosphorylases and starch synthetases are found in potato tuber, which are capable of utilizing reaction 1 product as primer for the synthesis of protein‐bound glucan. Copyright © 1987, Wiley Blackwell. All rights reserved
format JOUR
author MORENO, S.
CARDINI, C.E.
TANDECARZ, J.S.
author_facet MORENO, S.
CARDINI, C.E.
TANDECARZ, J.S.
author_sort MORENO, S.
title α‐Glucan synthesis on a protein primer: A reconstituted system for the formation of protein‐bound α‐glucan
title_short α‐Glucan synthesis on a protein primer: A reconstituted system for the formation of protein‐bound α‐glucan
title_full α‐Glucan synthesis on a protein primer: A reconstituted system for the formation of protein‐bound α‐glucan
title_fullStr α‐Glucan synthesis on a protein primer: A reconstituted system for the formation of protein‐bound α‐glucan
title_full_unstemmed α‐Glucan synthesis on a protein primer: A reconstituted system for the formation of protein‐bound α‐glucan
title_sort α‐glucan synthesis on a protein primer: a reconstituted system for the formation of protein‐bound α‐glucan
url http://hdl.handle.net/20.500.12110/paper_00142956_v162_n3_p609_MORENO
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