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IndexCopernicus Journal Abstract
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Effect of immobilization on the enzymes of glycogen metabolism. I Kalapos, A Szöör, G Vereb, G Bot, M Rapcsák, T Szilágyi Acta Physiol Hung 1983; 62(1):85-91 ICID: 168282 |
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| IC™ Value: 3.25 | ||
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| Activity of the enzymes regulating glycogen metabolism was determined forglycogen phosphorylase (Ph), phosphorylase kinase (PhK) and glycogen synthetase (GS) in fast extensordigitorum longus (EDL) and slow (soleus) muscles of rats following immobilization by plastering. It wasshown that the activity not only of Ph but also of PhK was about 8 times higher in the EDL than in thesoleus muscle in correlation with the higher glycogenolytic activity of fast muscles. The activity ofGS was approximately similar in the two muscles. PhK activity decreased significantly in the immobilizedEDL muscle while in the soleus an early reduction of GS activity ensued. Reduction of the activity ofthe glycogenolytic enzymes caused dedifferentiation in the muscles with anaerobic metabolism and containinglarge amounts of glycogenolytic enzymes. The similar rate of Ph and PhK in fast and slow muscles, aswell as the similar rate of their reduced activity, during immobilization indicated a close correlationbetween the two enzymes and raised the possibility of a combined regulation of their turnover. | ||
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ICID 168282 PMID 6417977 - click here to show this article in PubMed database |
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