Open AccessThe Rate of Release of ATP from Its Complex with Myosin
Author(s) -
CARDON Jeffrey W.,
BOYER Paul D.
Publication year - 1978
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1978.tb12765.x
Subject(s) - myosin , dissociation (chemistry) , chemistry , biophysics , adenosine triphosphate , reaction rate constant , dissociation constant , biochemistry , kinetics , biology , physics , classical mechanics , receptor
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 K d 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.