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. 1993 Mar 15;290(Pt 3):731–734. doi: 10.1042/bj2900731

Effects of different enzymic treatments on the release of titin fragments from rabbit skeletal myofibrils. Purification of an 800 kDa titin polypeptide.

C Astier 1, J P Labbé 1, C Roustan 1, Y Benyamin 1
PMCID: PMC1132341  PMID: 8457201

Abstract

In myofibrils, titin (also called connectin) molecules span from Z line to M line and constitute a third filament system containing an elastic domain in the I band. This giant protein is particularly sensitive to proteolysis in situ. Treatment of rabbit skeletal myofibrils with exogenous proteinases induces a release of titin fragments, which are detected in the soluble myofibrillar fraction. The cleavage of titin occurs at specific points localized at the proximity of Z line and could lead to a concomitant release of alpha-actinin.

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Selected References

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