Properties of Glycogen Synthetase in Erythrocytes

Shimon W. Moses, Nava Bashan, Alisa Gutman

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

Abstract

Erythrocyte glycogen synthetase activity was found to be absolutely dependent on the presence of glucose‐6‐phosphate (Glc‐6‐P). The Km, for UDPG and the Ka for Glc‐6‐P were not altered by preincubation of the enzyme. Glucose‐6‐phosphate protected the enzyme against thermal in‐act:ivation. Enzyme activity was inhibited by P1, SO4=, ATP, theophylline and caffeine. Galactose‐6‐phosphate could replace Glc‐6‐P as activator. A study to the effect of various combinations of Glc‐6‐P, ATP and P1 at concentrations prevailing in the red blood cell suggested that Glc‐6‐P concentration, rather than the effect of inhibitors, was the main factor limiting the activity of erythrocyte glycogen synthetase. The low rate of glycogen synthesis in erythrocytes can be related to the lack of conversion of the enzyme to a glucose‐6‐phosphate independent form.

Original languageEnglish
Pages (from-to)205-210
Number of pages6
JournalEuropean Journal of Biochemistry
Volume30
Issue number2
DOIs
StatePublished - 1 Jan 1972

ASJC Scopus subject areas

  • Biochemistry

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