Publication | Closed Access
Effects of different enzymic treatments on the release of titin fragments from rabbit skeletal myofibrils. Purification of an 800 kDa titin polypeptide
26
Citations
25
References
1993
Year
Titin FragmentsMolecular BiologyCytoskeletonCellular PhysiologySkeletal MuscleProtein FoldingZ LineMechanobiologyProtein FunctionMolecular PhysiologyBiochemistryProtein TransportKda Titin PolypeptideCell BiologyMycoproteinRabbit Skeletal MyofibrilsNatural SciencesPhysiologyBiotechnologyCell MotilityProtein EngineeringIntracellular TraffickingMedicineGiant Protein
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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