FILAMENT LENGTHS IN STRIATED MUSCLE

doi:10.1083/jcb.19.2.369

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ARTICLE

FILAMENT LENGTHS IN STRIATED MUSCLE

Sally G. Page ¹ and H. E. Huxley Ph.D¹

¹ From the Department of Biophysics, University College, London, England.

Dr. Huxley's present address is the Medical Research Council Laboratory for Molecular Biology, Cambridge, England

Filament lengths in resting and excited frog muscles have beenmeasured in the electron microscope, and investigations madeof the changes in length that are found under different conditions,to distinguish between those changes which arise during preparationand the actual differences in the living muscles. It is concludedthat all the measured differences in filament length are causedby the preparative procedures in ways that can be simply accountedfor, and that the filament lengths are the same in both restingand excited muscles at all sarcomere lengths greater than 2.1µ, viz., A filaments, 1.6 µ; I filaments, 2.05 µ.The fine periodicity visible along the I filaments also hasbeen measured in frog, toad, and rabbit muscles and found tobe 406 A.

Submitted on April 11, 1963

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Cohen, C., Longley, W. (1966). Tropomyosin Paracrystals Formed by Divalent Cations. Science 152: 794-796 [Abstract]
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