The study determined the binding constant of ATP to myosin subfragment 1 to be (3.25 +/- 0.96) X 10(11) M-1 under specific conditions.
No immediate clinical implications for cardiovascular practice; extends in vitro myosin biochemistry while leaving open translation to cardiac energetics.
The extent of ATP synthesis from ADP and Pi at the active centre of myosin subfragment 1 has been reinvestigated. The results have been interpreted using a treatment which is not dependent on the number or nature of the intermediates in the ATPase mechanism. An average value for the binding constant of ATP of (3.25 +/- 0.96) X 10(11) M-1 at pH 8.0 23 degrees C and ionic strength 0.12 M was obtained. Additional evidence is given to confirm that synthesis at the active site has been investigated.
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Goody et al. (1977) studied this question.
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