Abstract
The degree of polarization of the intrinsic tryptophan fluorescence of glycerinated single muscle fibres or fibre bundles (rabbit psoas or dorsal longitudinal muscle of Lethocerus maximus) was measured:
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a)
With sufficiently high (15 mM) ATP concentration or when an ATP regenerating system was used no difference in the degree of polarization of a contracting and a relaxed muscle was detected, whereas a distinct difference was detected between the relaxed and the rigor state. In contrast a distinct difference between the relaxed and contracting state was obtained at low ATP concentrations (5 mM). This difference is interpreted to be caused by an ATP-free core (rigor core) in the centre of the fibre.
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b)
No change in the polarization degree was detected after a rapid release of the contracting muscle.
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c)
In rigor state no difference in the degree of polarization of the tryptophan fluorescence was observed in the presence or absence of AMPPNP (concentration 0.5 mM).
These findings and the lack of difference between the polarization degree of the contracting and the relaxed muscle is interpreted to indicate that the polarization degree of the tryptophan fluorescence is not sensitive to the orientation of the cross bridges, or that the cross bridges do not rotate.
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Güth, K. Polarization of tryptophan fluorescence measurements in muscle. Biophys. Struct. Mechanism 6, 81–93 (1980). https://doi.org/10.1007/BF00535746
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DOI: https://doi.org/10.1007/BF00535746