Abstract
In horseshoe crab skeletal muscle fibers, the extension of SEC at the maximum isometric force P 0 is about 6% of the slack fiber length L 0 (sarcomere length, 7 μm), i.e., about 210 nm per half-sarcomere, being too large to be explained by the cross-bridge and the thin filament elasticities. Cinematographic studies of isometrically contracting myofibril bundes indicate that the highly compliant SEC mostly originates from the “elastic” thick filament misalignment in each A-band during isometric force generation. Possible contribution of the titin filaments to the “elastic” thick filament misalignment is discussed.
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Sugi, H., Akimoto, T., Kobayashi, T., Suzuki, S., Shimada, M. (2000). Possible Contribution of Titin Filaments to the Compliant Series Elastic Component in Horseshoe Crab Skeletal Muscle Fibers. In: Granzier, H.L., Pollack, G.H. (eds) Elastic Filaments of the Cell. Advances in Experimental Medicine and Biology, vol 481. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-4267-4_22
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DOI: https://doi.org/10.1007/978-1-4615-4267-4_22
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