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IS MUSCLE CONTRACTION ESSENTIALLY AN ENZYME-SUBSTRATE COMBINATION?

Nature volume 150, pages 4649 (11 July 1942) | Download Citation

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Abstract

ABOUT twelve months ago an account was given in NATURE of the striking action of adenylpyro-phosphate upon the flow-birefringence and viscous properties of the globulin of muscle, myosin1. Since the dephosphorylation of adenylpyrophosphate is believed to be the immediate source of energy for contraction, and since, in the most recent work, it has proved impossible, in spite of serious efforts, to separate adenylpyrophosphatase activity from the protein myosin (Bailey2, Needham8, confirming the original work of Engelhardt and Ljubimova4), a continuation of this work seemed necessary. Having in the meantime made further progress in the study of the physico-chemical relations of adenylpyrophosphate and myosin, we desire to make the following further interim report.

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Affiliations

  1. F.R.S., Biochemical Laboratory, Cambridge

    • JOSEPH NEEDHAM
  2. Biochemical Laboratory, Cambridge

    • ARNOŠT KLEINZELLER
    • , MARGARET MIALL
    • , MARY DAINTY
    • , DOROTHY M. NEEDHAM
    •  & A. S. C. LAWRENCE

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https://doi.org/10.1038/150046a0

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