On the enthalpy of binding of ADP to heavy meromyosin
- 1 January 1975
- journal article
- research article
- Published by Wiley in Journal of Supramolecular Structure
- Vol. 3 (4), 361-367
- https://doi.org/10.1002/jss.400030408
Abstract
The binding of ADP to heavy meromyosin has been studied by microcalorimetry. Minute amounts of myokinase interfere with binding measurements, but by selection of appropriate conditions, we can estimate that the value of the apparent ΔHbinding lies between −1.0 and −3.0 kcal per mole of ADP bound (0.3 M KCl, 2 mM MgCl2, 20 mM Tris, pH 8.00, 20°C). Values of ΔHbinding reported to date are an order of magnitude larger, and we suggest that these values are artifactual results due to myokinase contamination.Keywords
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