Abstract
IT has been previously reported that the synaeresis of actomyosin gels with adenosine triphosphate is accompanied by changes in the X-ray diffraction pattern indicating that some part of the actinmyosin complex undergoes supercontraction1. The recent observation by Goodall2 that one or more protons at each active site are involved in the production of tension in the myofibril is in line with my experiments, which suggest that the supercontraction of myosin (or actomyosin), long postulated as the fundamental basis of muscle contraction3, might also be due primarily to some specific transfer of protons.
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References
Pautard, F. G.E., Nature, 182, 788 (1958).
Goodall, M. C., Nature, 182, 677 (1958).
See, for example, Astbury, W. T., Proc. Roy. Soc., B, 134, 303 (1947) (Croonian Lecture, 1945).
Dubuisson, M., Arch. Intern. Physiol., 50, 203 (1940).
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PAUTARD, F. Proton Transfer and Supercontraction in Actomyosin. Nature 183, 1391–1392 (1959). https://doi.org/10.1038/1831391b0
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DOI: https://doi.org/10.1038/1831391b0
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