An approach previously published from this laboratory for measurement of the rate of dissociation of ATP from its complex with myosin has been carefully evaluated. The procedure has been found valid, and the off constant (21 °C, I= 0.21 M, pH 7.0) is 1 × 10−4 s−1. Other data for the rate of ATP binding give a Kd for myosin ATP of 6 × 10−11 M. Reasons for the apparent discrepancy between this value and thatreported by others have been examined. When various factors are appropriately taken into account, this discrepancy is eliminated. Copyright © 1978, Wiley Blackwell. All rights reserved
CITATION STYLE
CARDON, J. W., & BOYER, P. D. (1978). The Rate of Release of ATP from Its Complex with Myosin. European Journal of Biochemistry, 92(2), 443–448. https://doi.org/10.1111/j.1432-1033.1978.tb12765.x
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