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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1962
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00063002_v65_n2_p307_Krisman http://hdl.handle.net/20.500.12110/paper_00063002_v65_n2_p307_Krisman |
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paper:paper_00063002_v65_n2_p307_Krisman2023-06-08T14:30:53Z a-1,4-glucan: a-1,4-glucan 6-glycosyltransferase from liver Krisman de Fischman, Clara Rebeca 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. 1962 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00063002_v65_n2_p307_Krisman 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 de Fischman, Clara Rebeca 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. |
| author |
Krisman de Fischman, Clara Rebeca |
| author_facet |
Krisman de Fischman, Clara Rebeca |
| author_sort |
Krisman de Fischman, Clara Rebeca |
| 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 |
| publishDate |
1962 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00063002_v65_n2_p307_Krisman http://hdl.handle.net/20.500.12110/paper_00063002_v65_n2_p307_Krisman |
| work_keys_str_mv |
AT krismandefischmanclararebeca a14glucana14glucan6glycosyltransferasefromliver |
| _version_ |
1768543927025008640 |