Document Detail


Glycogenolysis during recovery from muscular work. The time course of phosphorylase activity is dependent on Pi concentration in the abdominal muscle of the shrimp Crangon crangon.
MedLine Citation:
PMID:  2775483     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
1) Glycogen is degraded in the abdominal muscle of the shrimp Crangon crangon (Decapoda, Crustacea) during the recovery period following work. The regulation of post-exercise glycogen breakdown and the properties of glycogen phosphorylase (EC 2.4.1.1) have been studied: 2) Glycogen phosphorylase exists as unphosphorylated b-form and phosphorylated a-form, the latter contains 1 molecule phosphate/subunit. Both forms of phosphorylase are dimers, isoenzymes have not been detected. 3) The purified b-form is inactive in absence of AMP and has very low affinities for AMP and Pi. For half-maximum activation 0.33 +/- 0.04 mM AMP is necessary, and the Km-value for Pi at 1 mM AMP is 48 +/- 5 mM. IMP does not affect the activity of the b-form. 4) The a-form is active without effectors, its Km-value for Pi is 5.3 +/- 1.5 mM. The proportion of phosphorylase a increases in vivo, from about 25% at rest, to approximately 90% upon work and remains at this high level during the first minutes of recovery. 5) It is concluded that the glycogenolytic flux in the abdominal muscle of the shrimp even during post-exercise periods depends on the level of the a-form the activity of which is restricted in time and extent by the cytoplasmic Pi concentration (Kamp, G. & Juretschke, H. P. (1987) Biochim. Biophys. Acta 929, 121-127).
Authors:
G Kamp
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biological chemistry Hoppe-Seyler     Volume:  370     ISSN:  0177-3593     ISO Abbreviation:  Biol. Chem. Hoppe-Seyler     Publication Date:  1989 Jun 
Date Detail:
Created Date:  1989-10-23     Completed Date:  1989-10-23     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  8503054     Medline TA:  Biol Chem Hoppe Seyler     Country:  GERMANY, WEST    
Other Details:
Languages:  eng     Pagination:  565-73     Citation Subset:  IM    
Affiliation:
Zoologisches Institut der Universität Münster.
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MeSH Terms
Descriptor/Qualifier:
Adenosine Monophosphate / physiology
Animals
Decapoda (Crustacea) / physiology*
Electric Stimulation
Glycogen / metabolism*
Inosine Monophosphate / physiology
Isoenzymes / analysis
Kinetics
Muscles / physiology
Phosphates / physiology
Phosphorylase Kinase
Phosphorylases / isolation & purification,  metabolism*
Phosphorylation
Chemical
Reg. No./Substance:
0/Isoenzymes; 0/Phosphates; 131-99-7/Inosine Monophosphate; 61-19-8/Adenosine Monophosphate; 9005-79-2/Glycogen; EC 2.4.1.-/Phosphorylases; EC 2.7.1.19/Phosphorylase Kinase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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