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. 1974 Feb;71(2):274–277. doi: 10.1073/pnas.71.2.274

The Site of Force Generation in Muscle Contraction as Deduced from Fluorescence Polarization Studies

T Nihei 1, Robert A Mendelson 1, Jean Botts 1
PMCID: PMC387985  PMID: 4521799

Abstract

The fluorescent dye, N(-iodoacetylamino)-l-naphthylanine-5-sulfonic acid, labeled exclusively the myosin cross-bridges in rabbit glycerinated psoas muscle fibers, without impairing their function. Fluorescence polarization was used to study cross-bridge orientation in rigor, relaxation, and contraction, as a function of sarcomere length. At a length where no overlap between thick and thin filaments occurs, rigor-inducing, relaxation-inducing, and contraction-inducing solutions all induced the relaxation attitude. At lengths where overlap does exist, the slowly-hydrolyzing ATP analog, “α,β-methylene ATP,” induced the relaxation attitude. The data were consistent with the A. F. Huxley-Simmons model of force generation. Combined with our earlier results, the data indicated that torque was generated at the actin-myosin interface.

Keywords: psoas, cross-bridge, myofilament, overlap, myosin

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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