α‐Glucan synthesis on a protein primer, uridine diphosphoglucose: protein transglucosylase I: Separation from starch synthetase and phosphorylase and a study of its properties
It was found that the DEAE‐cellulose‐treated UDP‐Glc:protein transglucosylase I catalyzing the first step (reaction 1) in the formation of α‐glucan bound to protein in potato tuber is not only specific for the glucosyl donor but also for the endogenous acceptor. A single radioactive 38‐kDa macromole...
Guardado en:
| Autores principales: | , |
|---|---|
| Publicado: |
1986
|
| Materias: | |
| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00142956_v157_n3_p539_MORENO http://hdl.handle.net/20.500.12110/paper_00142956_v157_n3_p539_MORENO |
| Aporte de: |
| id |
paper:paper_00142956_v157_n3_p539_MORENO |
|---|---|
| record_format |
dspace |
| spelling |
paper:paper_00142956_v157_n3_p539_MORENO2023-06-08T14:36:39Z α‐Glucan synthesis on a protein primer, uridine diphosphoglucose: protein transglucosylase I: Separation from starch synthetase and phosphorylase and a study of its properties Moreno, Silvia Tandecarz, Juana Sara 1,4 glucan 1,4-glucan alpha 1,4 glucan protein synthase (UDP forming) alpha-1,4-glucan-protein synthase (UDP-forming) amino acid glucan glucosyltransferase serine threonine vegetable protein article biosynthesis chromatography enzyme specificity enzymology isolation and purification kinetics metabolism plant polyacrylamide gel electrophoresis potato Amino Acids Chromatography Electrophoresis, Polyacrylamide Gel Glucans Glucosyltransferases Kinetics Plant Proteins Plants Potatoes Serine Substrate Specificity Support, Non-U.S. Gov't Threonine It was found that the DEAE‐cellulose‐treated UDP‐Glc:protein transglucosylase I catalyzing the first step (reaction 1) in the formation of α‐glucan bound to protein in potato tuber is not only specific for the glucosyl donor but also for the endogenous acceptor. A single radioactive 38‐kDa macromolecular component appeared during denaturing polyacrylamide gel electrophoresis of reaction 1 product. The labeled component is probably the polypeptide subunit of the endogenous acceptor which is being glucosylated. The radioactivity incorporated in reaction 1 product was isolated from a protease digest as a low‐molecular‐mass glucopeptide fraction. A β‐elimination reaction carried out in the presence of a reducing agent demonstrated that only one glucosyl moiety is transferred from UDP‐Glc to the aminoacyl residue, thus forming an O‐glucosidic linkage. 3H‐labeled sodium borohydride showed that serine and threonine are involved in the peptide bond to glucose. Ion‐exchange chromatography on DEAE‐cellulose, affinity chromatography on concanavalin‐A—Sepharose, gel filtration on Sephacryl S‐300 and sucrose density gradient centrifugation failed to separate the enzyme catalyzing reaction 1 from the endogenous acceptor. Copyright © 1986, 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. 1986 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00142956_v157_n3_p539_MORENO http://hdl.handle.net/20.500.12110/paper_00142956_v157_n3_p539_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 alpha 1,4 glucan protein synthase (UDP forming) alpha-1,4-glucan-protein synthase (UDP-forming) amino acid glucan glucosyltransferase serine threonine vegetable protein article biosynthesis chromatography enzyme specificity enzymology isolation and purification kinetics metabolism plant polyacrylamide gel electrophoresis potato Amino Acids Chromatography Electrophoresis, Polyacrylamide Gel Glucans Glucosyltransferases Kinetics Plant Proteins Plants Potatoes Serine Substrate Specificity Support, Non-U.S. Gov't Threonine |
| spellingShingle |
1,4 glucan 1,4-glucan alpha 1,4 glucan protein synthase (UDP forming) alpha-1,4-glucan-protein synthase (UDP-forming) amino acid glucan glucosyltransferase serine threonine vegetable protein article biosynthesis chromatography enzyme specificity enzymology isolation and purification kinetics metabolism plant polyacrylamide gel electrophoresis potato Amino Acids Chromatography Electrophoresis, Polyacrylamide Gel Glucans Glucosyltransferases Kinetics Plant Proteins Plants Potatoes Serine Substrate Specificity Support, Non-U.S. Gov't Threonine Moreno, Silvia Tandecarz, Juana Sara α‐Glucan synthesis on a protein primer, uridine diphosphoglucose: protein transglucosylase I: Separation from starch synthetase and phosphorylase and a study of its properties |
| topic_facet |
1,4 glucan 1,4-glucan alpha 1,4 glucan protein synthase (UDP forming) alpha-1,4-glucan-protein synthase (UDP-forming) amino acid glucan glucosyltransferase serine threonine vegetable protein article biosynthesis chromatography enzyme specificity enzymology isolation and purification kinetics metabolism plant polyacrylamide gel electrophoresis potato Amino Acids Chromatography Electrophoresis, Polyacrylamide Gel Glucans Glucosyltransferases Kinetics Plant Proteins Plants Potatoes Serine Substrate Specificity Support, Non-U.S. Gov't Threonine |
| description |
It was found that the DEAE‐cellulose‐treated UDP‐Glc:protein transglucosylase I catalyzing the first step (reaction 1) in the formation of α‐glucan bound to protein in potato tuber is not only specific for the glucosyl donor but also for the endogenous acceptor. A single radioactive 38‐kDa macromolecular component appeared during denaturing polyacrylamide gel electrophoresis of reaction 1 product. The labeled component is probably the polypeptide subunit of the endogenous acceptor which is being glucosylated. The radioactivity incorporated in reaction 1 product was isolated from a protease digest as a low‐molecular‐mass glucopeptide fraction. A β‐elimination reaction carried out in the presence of a reducing agent demonstrated that only one glucosyl moiety is transferred from UDP‐Glc to the aminoacyl residue, thus forming an O‐glucosidic linkage. 3H‐labeled sodium borohydride showed that serine and threonine are involved in the peptide bond to glucose. Ion‐exchange chromatography on DEAE‐cellulose, affinity chromatography on concanavalin‐A—Sepharose, gel filtration on Sephacryl S‐300 and sucrose density gradient centrifugation failed to separate the enzyme catalyzing reaction 1 from the endogenous acceptor. Copyright © 1986, Wiley Blackwell. All rights reserved |
| author |
Moreno, Silvia Tandecarz, Juana Sara |
| author_facet |
Moreno, Silvia Tandecarz, Juana Sara |
| author_sort |
Moreno, Silvia |
| title |
α‐Glucan synthesis on a protein primer, uridine diphosphoglucose: protein transglucosylase I: Separation from starch synthetase and phosphorylase and a study of its properties |
| title_short |
α‐Glucan synthesis on a protein primer, uridine diphosphoglucose: protein transglucosylase I: Separation from starch synthetase and phosphorylase and a study of its properties |
| title_full |
α‐Glucan synthesis on a protein primer, uridine diphosphoglucose: protein transglucosylase I: Separation from starch synthetase and phosphorylase and a study of its properties |
| title_fullStr |
α‐Glucan synthesis on a protein primer, uridine diphosphoglucose: protein transglucosylase I: Separation from starch synthetase and phosphorylase and a study of its properties |
| title_full_unstemmed |
α‐Glucan synthesis on a protein primer, uridine diphosphoglucose: protein transglucosylase I: Separation from starch synthetase and phosphorylase and a study of its properties |
| title_sort |
α‐glucan synthesis on a protein primer, uridine diphosphoglucose: protein transglucosylase i: separation from starch synthetase and phosphorylase and a study of its properties |
| publishDate |
1986 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00142956_v157_n3_p539_MORENO http://hdl.handle.net/20.500.12110/paper_00142956_v157_n3_p539_MORENO |
| work_keys_str_mv |
AT morenosilvia aglucansynthesisonaproteinprimeruridinediphosphoglucoseproteintransglucosylaseiseparationfromstarchsynthetaseandphosphorylaseandastudyofitsproperties AT tandecarzjuanasara aglucansynthesisonaproteinprimeruridinediphosphoglucoseproteintransglucosylaseiseparationfromstarchsynthetaseandphosphorylaseandastudyofitsproperties |
| _version_ |
1768544622504574976 |