The formation of branched glucans in sweet corn

The properties of a preparation of α-glucan branching glycosyl transferase (α-1,4-glucan:α-1, 4-glucan 6-glycosyltransferase E.C. 2.4.1.18) from sweet corn were studied by using amylose and amylopectin as substrates. The preparation behaved differently toward each substrate, with respect to pH optim...

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Detalles Bibliográficos
Autor principal:	Lavintman, Nelly
Publicado:	1966
Materias:	citric acid glucosyltransferase mercury pectin plant extract polysaccharide animal article biosynthesis cereal chemistry electron microscopy enzymology liver maize pH rabbit temperature wheat Animal Cereals Chemistry Citrates Glucosyltransferases Hydrogen-Ion Concentration Liver Mercury Microscopy, Electron Pectins Plant Extracts Polysaccharides Rabbits Temperature Triticum Zea mays
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v116_nC_p1_Lavintman http://hdl.handle.net/20.500.12110/paper_00039861_v116_nC_p1_Lavintman
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_00039861_v116_nC_p1_Lavintman
record_format	dspace
spelling	paper:paper_00039861_v116_nC_p1_Lavintman2023-06-08T14:24:52Z The formation of branched glucans in sweet corn Lavintman, Nelly citric acid glucosyltransferase mercury pectin plant extract polysaccharide animal article biosynthesis cereal chemistry electron microscopy enzymology liver maize pH rabbit temperature wheat Animal Cereals Chemistry Citrates Glucosyltransferases Hydrogen-Ion Concentration Liver Mercury Microscopy, Electron Pectins Plant Extracts Polysaccharides Rabbits Temperature Triticum Zea mays The properties of a preparation of α-glucan branching glycosyl transferase (α-1,4-glucan:α-1, 4-glucan 6-glycosyltransferase E.C. 2.4.1.18) from sweet corn were studied by using amylose and amylopectin as substrates. The preparation behaved differently toward each substrate, with respect to pH optimum, activation by citrate, and the effect of Hg++ and temperature. Similar extracts obtained from starchy maize, wheat, and barley were shown to have only Q-enzyme activity i.e., no action on amylopectin. Studies on substrate specificity showed that maltodextrins of average DP2 2 DP: degree of polymerization. above 22 served as substrates for sweet corn, starchy maize, and liver branching preparations. Electron micrographs of natural phytoglycogen are shown. © 1966. Fil:Lavintman, N. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1966 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v116_nC_p1_Lavintman http://hdl.handle.net/20.500.12110/paper_00039861_v116_nC_p1_Lavintman
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	citric acid glucosyltransferase mercury pectin plant extract polysaccharide animal article biosynthesis cereal chemistry electron microscopy enzymology liver maize pH rabbit temperature wheat Animal Cereals Chemistry Citrates Glucosyltransferases Hydrogen-Ion Concentration Liver Mercury Microscopy, Electron Pectins Plant Extracts Polysaccharides Rabbits Temperature Triticum Zea mays
spellingShingle	citric acid glucosyltransferase mercury pectin plant extract polysaccharide animal article biosynthesis cereal chemistry electron microscopy enzymology liver maize pH rabbit temperature wheat Animal Cereals Chemistry Citrates Glucosyltransferases Hydrogen-Ion Concentration Liver Mercury Microscopy, Electron Pectins Plant Extracts Polysaccharides Rabbits Temperature Triticum Zea mays Lavintman, Nelly The formation of branched glucans in sweet corn
topic_facet	citric acid glucosyltransferase mercury pectin plant extract polysaccharide animal article biosynthesis cereal chemistry electron microscopy enzymology liver maize pH rabbit temperature wheat Animal Cereals Chemistry Citrates Glucosyltransferases Hydrogen-Ion Concentration Liver Mercury Microscopy, Electron Pectins Plant Extracts Polysaccharides Rabbits Temperature Triticum Zea mays
description	The properties of a preparation of α-glucan branching glycosyl transferase (α-1,4-glucan:α-1, 4-glucan 6-glycosyltransferase E.C. 2.4.1.18) from sweet corn were studied by using amylose and amylopectin as substrates. The preparation behaved differently toward each substrate, with respect to pH optimum, activation by citrate, and the effect of Hg++ and temperature. Similar extracts obtained from starchy maize, wheat, and barley were shown to have only Q-enzyme activity i.e., no action on amylopectin. Studies on substrate specificity showed that maltodextrins of average DP2 2 DP: degree of polymerization. above 22 served as substrates for sweet corn, starchy maize, and liver branching preparations. Electron micrographs of natural phytoglycogen are shown. © 1966.
author	Lavintman, Nelly
author_facet	Lavintman, Nelly
author_sort	Lavintman, Nelly
title	The formation of branched glucans in sweet corn
title_short	The formation of branched glucans in sweet corn
title_full	The formation of branched glucans in sweet corn
title_fullStr	The formation of branched glucans in sweet corn
title_full_unstemmed	The formation of branched glucans in sweet corn
title_sort	formation of branched glucans in sweet corn
publishDate	1966
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v116_nC_p1_Lavintman http://hdl.handle.net/20.500.12110/paper_00039861_v116_nC_p1_Lavintman
work_keys_str_mv	AT lavintmannelly theformationofbranchedglucansinsweetcorn AT lavintmannelly formationofbranchedglucansinsweetcorn
_version_	1768546700803178496

The formation of branched glucans in sweet corn

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