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Affinity of glycogen synthetase to crosslinked glycogen
Author(s) -
Zemek J.,
Bauer Š.,
Kuniak Ľ.
Publication year - 1979
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1979.360180905
Subject(s) - glycogen , glycogen branching enzyme , chemistry , glycogen synthase , yeast , glycogen debranching enzyme , biochemistry , glycogenesis , glycogen phosphorylase , uridine diphosphate glucose , uridine , enzyme , rna , gene
The affinity of yeast glycogen synthetase to glycogen modified by crosslinking has been studied under various experimental conditions. It was found that the higher the degree of crosslinking, the lower the affinity of glycogen synthetase to glycogen. The amount of glycogen synthetase adsorbed from the solution depends on the amount of crosslinked glycogen added and is inversely proportional to the concentration of the soluble glycogen. The stability of the complex formed between yeast glycogen synthetase and the crosslinked glycogen was found to be maximal at neutral pH range. The presence of glucose 6‐phosphate, uridine 5′‐di‐phosphate, and uridine 5′‐diphosphate glucose enhanced the stability of the complex.