An activity staining method of α-1,4-glucan branching enzyme by the cooperative action with glycogen phosphorylase immobilized within polyacrylamide gels
- 1 October 1980
- journal article
- research article
- Published by Elsevier in Analytical Biochemistry
- Vol. 108 (1), 16-24
- https://doi.org/10.1016/0003-2697(80)90688-0
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- A new glycogen phosphorylase present in the rat tissues containing the brain‐type isozymeFEBS Letters, 1978
- De Novo synthesis of Escherichia coli glycogen is due to primer associated with glycogen synthase and activation by branching enzymeArchives of Biochemistry and Biophysics, 1978
- Combined action of Escherichia coli glycogen synthase and branching enzyme in the so-called “unprimed” polyglucoside synthesisArchives of Biochemistry and Biophysics, 1978
- A primer independent activity of rabbit muscle phosphorylasebMolecular and Cellular Biochemistry, 1977
- The initiation of glycogen biosynthesis inEscherichia coliFEBS Letters, 1975
- A Precursor of Glycogen Biosynthesis: α‐1,4‐Glucan‐ProteinEuropean Journal of Biochemistry, 1975
- Unprimed glucan biosynthesis by a particulate ADP-glucose-glucan glucosyl transferase from an Escherichia coli mutant and its stimulation by a protein factorBiochemical and Biophysical Research Communications, 1973
- Purification and properties of rat muscle glycogen phosphorylaseBiochemistry, 1969
- Enzyme system for de novo biosynthesis of glycogen in Aerobacter aerogenesBiochemistry, 1968
- A method for the colorimetric estimation of glycogen with lodineAnalytical Biochemistry, 1962