Free and bound nucleotides in frog and mammalian muscle

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Abstract

The Atp of muscle can be separated into three fractions by differential extraction of the powered frozen muscle. A fraction firmly bound to protein, equivalent to 5–6 moles/mole of myosin in bullfrogs, and to more than twice this amount in cats, is considered to act as the bridge between myosin and actin necessary to account for the structure of resting striated muscle shown by the electron microscope. A second fraction is also considered to be protein-bound, but, fairly readily dissociable therefrom. More ATP is found unbound to protein in bullfrog than in cat muscle. The ADP in both species is essentially all protein-bound and is present in an amount equivalent to the 1 mole/mole of F-actin monomer that has been found for the isolated protein. Tetanic contraction of 15 seconds duration does not lead to any significant change in relations between free and bound nucleotide derivatives.

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This work was supported in part by grant AM 07273 from the National Institute of Arthritis and Metabolic diseases, and in part by a National Science Foundation grant to this department for an Undergraduate Research Participation Program.

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