The Effect of Glucose and Glucose Analogues on the Conversion of Glycogen Synthetase from Phosphorylated to Dephosphorylated Form in Human Polymorphonuclear Leukocytes
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1972.tb01839.x/fullpdf
Reference26 articles.
1. Studies on UDPG-Glycogen Transglucosylase. I. Preparation and Differentiation of Two Activities of UDPG-Glycogen Transglucosylase from Rat Skeletal Muscle*
2. Studies on UDPG-α-Glucan Transglucosylase. III. Interconversion of Two Forms of Muscle UDPG-α-Glucan Transglucosylase by a Phosphorylation-Dephosphorylation Reaction Sequence*
3. Conversion of UDPG-α-glucan transglucosylase from glucose 6-phosphate dependent to independent activity in liver
4. Inactivation of Glycogen Synthetase and Activation of Phosphorylase Kinase by Muscle Adenosine 3',5'-Monophosphate-dependent Protein Kinases
5. An on-off mechanism for liver glycogen synthetase activity.
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1. Glucose-induced glycogenesis in the liver involves the glucose-6-phosphate-dependent dephosphorylation of glycogen synthase;Biochemical Journal;1997-03-15
2. New insight into the regulation of liver glycogen metabolism by glucose;Biochemical Society Transactions;1997-02-01
3. Demonstration of a Glycogen/Glucose 1-Phosphate Cycle in Hepatocytes from Fasted Rats;Journal of Biological Chemistry;1995-08
4. Rate and duration of net glycogen synthesis following glucose administration to fasted human leukocytes;FEBS Letters;1984-07-09
5. Activation of glycogen synthase in leukocytes is inhibited by the intracellular Ca-antagonist TMB-8;Biochemical and Biophysical Research Communications;1982-05
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