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. 1971 Mar;213(2):455–474. doi: 10.1113/jphysiol.1971.sp009393

The transformation of myosin in cross-innervated rat muscles

M Bárány, R I Close
PMCID: PMC1331771  PMID: 4252498

Abstract

1. The characteristics of isometric twitch and tetanic contractions have been determined for normal (N-EDL, N-SOL), self-innervated (S-EDL, S-SOL) and cross-innervated (X-EDL, X-SOL) extensor digitorum longus (EDL) and soleus (SOL) muscles of the rat at 35° C. The muscles were then used for biochemical analyses of properties of myosin and actomyosin.

2. The ATPase activities of myosin and actomyosin of X-EDL decreased to the level of those of N-SOL or S-SOL, and the ATPase activities of X-SOL approached those of N-EDL or S-EDL. Of the various ATPase activities, the actin- and Mg2+-activated ATPase activity of myosin and the Mg2+-activated ATPase activity of actomyosin showed the highest degree of correlation with the intrinsic speed of shortening of the muscles.

3. Myosin of normal, self-innervated, and cross-innervated muscles combined with F-actin superprecipitated at rates which were proportional to the speed of muscle contraction.

4. The pH profile curve and the ATP-induced dinitrophenylation reaction revealed that the structure of myosin of X-EDL was altered to that of N-SOL or S-SOL, and the structure of myosin of X-SOL was modified to that of N-EDL or S-EDL.

5. No differences were found in the yield of myosin of normal, self-innervated, and cross-innervated extensor digitorum longus and soleus muscles.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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