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[Changes in structural and functional properties of actin in denervated rabbit skeletal muscles].

Amino acid composition of actin from white skeletal muscles of the rabbit was studied 14 and 50 days after denervation. The content of valine, histidine and tyrosine was shown to decrease and that of lysine and leucine to increase on the 14th day following denervation. The content of these amino acids was almost normalised on the 50th day. In case of actin obtained from the contralateral leg similar but less pronounced changes were revealed. The results obtained are discussed as to the role played by some of amino acids in actin polymerization.