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.
| Documento: | Artículo |
| Título: | a-1,4-glucan: a-1,4-glucan 6-glycosyltransferase from liver |
| Autor: | Krisman, C.R. |
| Filiación: | Instituto de Investigaciones Bioquimicas Fundacion Campomar, Facultad de Ciencias Exactas y Naturales, Buenos Aires, Argentina |
| Palabras clave: | glucosyltransferase; article; liver; GLUCOSYLTRANSFERASES; LIVER; Glucosyltransferases; Liver |
| Año: | 1962 |
| Volumen: | 65 |
| Número: | 2 |
| Página de inicio: | 307 |
| Página de fin: | 315 |
| DOI: | http://dx.doi.org/10.1016/0006-3002(62)91049-1 |
| Título revista: | BBA - Biochimica et Biophysica Acta |
| ISSN: | 00063002 |
| CAS: | glucosyltransferase, 9031-48-5; Glucosyltransferases, 2.4.1.- |
| Registro: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00063002_v65_n2_p307_Krisman |
