a-1,4-glucan: a-1,4-glucan 6-glycosyltransferase from liver

a-1,4-glucan:a-1,4-glucan 6-glycosyltransferase was purified about 35-fold from rat-liver extracts. Removal of α-amylase could be accomplished by high-speed centrifugation of extracts from livers with high glycogen content. Enzyme action on amylopectin is optimum at pH 6.4 in 0.3 M citrate buffer. I...

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Autor principal: Krisman, C.R.
Formato: JOUR
Materias:
glucosyltransferase
article
liver
GLUCOSYLTRANSFERASES
LIVER
Glucosyltransferases
Liver
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00063002_v65_n2_p307_Krisman
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id todo:paper_00063002_v65_n2_p307_Krisman
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spelling todo:paper_00063002_v65_n2_p307_Krisman2023-10-03T14:04:40Z a-1,4-glucan: a-1,4-glucan 6-glycosyltransferase from liver Krisman, C.R. glucosyltransferase article liver GLUCOSYLTRANSFERASES LIVER Glucosyltransferases Liver a-1,4-glucan:a-1,4-glucan 6-glycosyltransferase was purified about 35-fold from rat-liver extracts. Removal of α-amylase could be accomplished by high-speed centrifugation of extracts from livers with high glycogen content. Enzyme action on amylopectin is optimum at pH 6.4 in 0.3 M citrate buffer. It requires salts for maximal activity, and is inhibited by molybdate, Mn2+, Mg2+ and sodium p-chloromercuribenzoate. Amylose and amylopectin ß-limit dextrin were also substrates for the liver branching enzyme. A method is described for the assay of the enzyme in the presence of α-amylase. © 1962. 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_00063002_v65_n2_p307_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 glucosyltransferase
article
liver
GLUCOSYLTRANSFERASES
LIVER
Glucosyltransferases
Liver
spellingShingle glucosyltransferase
article
liver
GLUCOSYLTRANSFERASES
LIVER
Glucosyltransferases
Liver
Krisman, C.R.
a-1,4-glucan: a-1,4-glucan 6-glycosyltransferase from liver
topic_facet glucosyltransferase
article
liver
GLUCOSYLTRANSFERASES
LIVER
Glucosyltransferases
Liver
description a-1,4-glucan:a-1,4-glucan 6-glycosyltransferase was purified about 35-fold from rat-liver extracts. Removal of α-amylase could be accomplished by high-speed centrifugation of extracts from livers with high glycogen content. Enzyme action on amylopectin is optimum at pH 6.4 in 0.3 M citrate buffer. It requires salts for maximal activity, and is inhibited by molybdate, Mn2+, Mg2+ and sodium p-chloromercuribenzoate. Amylose and amylopectin ß-limit dextrin were also substrates for the liver branching enzyme. A method is described for the assay of the enzyme in the presence of α-amylase. © 1962.
format JOUR
author Krisman, C.R.
author_facet Krisman, C.R.
author_sort Krisman, C.R.
title a-1,4-glucan: a-1,4-glucan 6-glycosyltransferase from liver
title_short a-1,4-glucan: a-1,4-glucan 6-glycosyltransferase from liver
title_full a-1,4-glucan: a-1,4-glucan 6-glycosyltransferase from liver
title_fullStr a-1,4-glucan: a-1,4-glucan 6-glycosyltransferase from liver
title_full_unstemmed a-1,4-glucan: a-1,4-glucan 6-glycosyltransferase from liver
title_sort a-1,4-glucan: a-1,4-glucan 6-glycosyltransferase from liver
url http://hdl.handle.net/20.500.12110/paper_00063002_v65_n2_p307_Krisman
work_keys_str_mv AT krismancr a14glucana14glucan6glycosyltransferasefromliver
_version_ 1807315920935190528

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