Since new methods to isolate connectin or titin in a native state have been published, it has become important to reinvestigate the role of connectin (titin) in meat tenderization during postmortem storage. In this paper, the isolation of native connectin from rabbit skeletal muscle (L. dorsi) was carried out, and postmortem changes in native connectin were studied quantitatively and qualitatively.
On the basis of the amino acid composition and electrophoretic mobility on sodium dodecyl sulfate-polyacrylamide gel, it is shown that the isolated protein was a highly pure connectin. An increase of the extractability of native connectin from the muscle during storage was observed, and an electron microscopic study of the purified native connectin indicates a qualitative change of connectin in the muscle during postmortem storage.
If connectin has some influence on meat tenderness, the quantitative and qualitative changes of native connectin in the muscle are possibly one of the cause of meat tenderization during conditioning.

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