Possibility of metabolite control of liver glycogen synthetase activity

Biochemistry ◽  
1970 ◽  
Vol 9 (4) ◽  
pp. 946-952 ◽  
Author(s):  
Alvin H. Gold
Keyword(s):  
Liver Glycogen ◽  
Synthetase Activity ◽  
Glycogen Synthetase

scholarly journals Depletion of glycogen synthetase and increase of glucose 6-phosphate dehydrogenase in livers of ethionine-treated mice

1965 ◽  
Vol 97 (1) ◽  
pp. 32-36 ◽  
Author(s):  
HG Sie ◽  
A Hablanian
Keyword(s):  
Pyruvate Kinase ◽  
Glucose Dehydrogenase ◽  
Liver Glycogen ◽  
Synthetase Activity ◽  
Phosphogluconate Dehydrogenase ◽  
Glycogen Synthetase ◽  
Glucose 6 Phosphate Dehydrogenase

1. Ethionine-treated mice showed a marked depletion in liver glycogen, a decrease of glycogen-synthetase activity, an increase in activity of glucose 6-phosphate dehydrogenase and the solubilization of phosphorylase. 2. The administration of cortisol or glucose did not alleviate these changes but the effect of ethionine was completely prevented in animals given methionine as well as ethionine. 3. The activities of the following enzymes were unchanged: hexokinase, glucokinase, glucose 6-phosphatase, phosphoglucomutase, 6-phosphogluconate dehydrogenase, UDP-glucose pyrophosphorylase, UDP-glucose dehydrogenase and pyruvate kinase.

Utilization of native primer by mammalian liver glycogen synthetase: primer efficiency in binding the enzyme and in catalysis

1968 ◽  
Vol 46 (6) ◽  
pp. 579-586 ◽  
Author(s):  
A. Vardanis
Keyword(s):  
Low Temperatures ◽  
Liver Glycogen ◽  
Catalytic Site ◽  
Lower Amount ◽  
Synthetase Activity ◽  
Substrate Complex ◽  
Glycogen Synthetase ◽  
Enzyme Substrate ◽  
Dependent Activity ◽  
Mammalian Liver

The particulate glycogen–glycogen synthetase complex isolated from mammalian liver is often strongly dependent on the addition of primer for activity. The present experiments offer an explanation for this behavior. Hepatic α-amylase, which is also adsorbed on the particle, can, even at the low temperatures (0–4°) of the preparatory procedure, hydrolyze the outer branches of particulate glycogen and thus reduce its efficiency as a primer. Synthetase activity of particulate glycogen prepared from the livers of starved animals is much more dependent on the addition of exogenous primer as compared to the enzyme from fed animals. Correspondingly, the livers of starved animals contain a lower amount of particulate glycogen and exhibit higher α-amylase activity.When particulate glycogen is rapidly prepared from fed animals, the glucose-6-P independent portion of its glycogen synthetase activity is only slightly increased by addition of extra primer. The glucose-6-P dependent activity of the same preparations, however, is doubled by addition of soluble glycogen, suggesting that the latter form of the synthetase is bound to glycogen in a partially inactive complex.The efficiency of a glycogen sample in binding the synthetase seems to be proportional to the ability of that sample to act as primer in the synthetase reaction. This finding strengthens the hypothesis that the enzyme is adsorbed to glycogen through its catalytic site, i.e. in an enzyme–substrate complex. It is evident, however, that in a number of cases this complex is only partially active since it exhibits varying degrees of dependence on added soluble primer.

scholarly journals Factors Affecting Muscle Glycogen Synthetase Activity

1967 ◽  
Vol 242 (6) ◽  
pp. 1227-1231
Author(s):  
Enrique Belocopitow ◽  
Maria del Carmen Garcia Fernandez ◽  
Lutz Birnbaumer ◽  
Héctor N. Torres
Keyword(s):  
Muscle Glycogen ◽  
Synthetase Activity ◽  
Factors Affecting ◽  
Glycogen Synthetase

scholarly journals Regulation of Rat Liver Glycogen Synthetase

1973 ◽  
Vol 248 (5) ◽  
pp. 1550-1555
Author(s):  
Michael J. Ernest ◽  
Ki-Han Kim
Keyword(s):  
Rat Liver ◽  
Liver Glycogen ◽  
Glycogen Synthetase

The Control of Liver Glycogen Synthetase Phosphatase by Phosphorylase

1971 ◽  
Vol 18 (4) ◽  
pp. 582-587 ◽  
Author(s):  
Willy Stalmans ◽  
Henri De Wulf ◽  
Henri-Gery Hers
Keyword(s):  
Liver Glycogen ◽  
Glycogen Synthetase

UDPG-glycogen synthetase activity in human leucocytes

1968 ◽  
Vol 158 (3) ◽  
pp. 465-467 ◽  
Author(s):  
Hibbard E. Williams ◽  
Ulla I. Lundholm
Keyword(s):  
Synthetase Activity ◽  
Glycogen Synthetase
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