Experimental investigations on hypokinesis of skeletal muscles with different function. IV. Changes in the sarcoplasmic proteins

Abstract

The changes in the sarcoplasmic proteins of the m. gastrocnemius and m. soleus were examined by biochemical methods on the 5th, 7th, 14th and 28th days after plaster cast immobilization of the right hind limbs of adult rabbits. During 4 weeks the soluble/myofibrillar protein ratio increased from 0.47 to 0.75 in the m. gastrocnemius, and to 0.85 in the m. soleus. Evaluation of the relative quantities of the components identified after gel-electrophoresis separation led to the following results: (1) There was no, or no appreciable change in the glyceraldehyde-3-phosphate dehydrogenase, creatine kinase and enolase activities. (2) The enzymes lactate dehydrogenase, aldolase and the glycogenolytic enzymes showed a relative decrease in both muscles. (3) Phosphoglycerate kinase, phosphoglucose isomerase and pyruvate kinase increased in both muscles. (4) Changes of opposite directions were exhibited by myoglobin, myokinase and F-protein. These results provide new data on the biochemical characterization of these functionally different muscles, and on the mechanism of disuse atrophy.