Kalapos I, Szöör A, Vereb G, Bot G, Rapcsák M, Szilágyi T
Acta Physiol Hung. 1983;62(1):85-91.
Activity of the enzymes regulating glycogen metabolism was determined for glycogen phosphorylase (Ph), phosphorylase kinase (PhK) and glycogen synthetase (GS) in fast extensor digitorum longus (EDL) and slow (soleus) muscles of rats following immobilization by plastering. It was shown that the activity not only of Ph but also of PhK was about 8 times higher in the EDL than in the soleus muscle in correlation with the higher glycogenolytic activity of fast muscles. The activity of GS was approximately similar in the two muscles. PhK activity decreased significantly in the immobilized EDL muscle while in the soleus an early reduction of GS activity ensued. Reduction of the activity of the glycogenolytic enzymes caused dedifferentiation in the muscles with anaerobic metabolism and containing large amounts of glycogenolytic enzymes. The similar rate of Ph and PhK in fast and slow muscles, as well as the similar rate of their reduced activity, during immobilization indicated a close correlation between the two enzymes and raised the possibility of a combined regulation of their turnover.
