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
This publication has 11 references indexed in Scilit:
- Thermal transitions of myosin and its helical fragments. I. Shifts in proton equilibriums accompanying unfoldingBiochemistry, 1975
- The characterization of myosin–product complexes and of product-release steps during the magnesium ion-dependent adenosine triphosphatase reactionBiochemical Journal, 1974
- Calorimetric studies of the binding of ligands to aldolaseBiochemistry, 1973
- A kinetic study of the energy storing enzyme-product complex in the hydrolysis of ATP by heavy meromyosinBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1973
- The reversibility of adenosine triphosphate cleavage by myosinBiochemical Journal, 1973
- Mechanism of adenosine triphosphate hydrolysis by actomyosinBiochemistry, 1971
- Equilibrium binding of adenosine diphosphate to myosinBiochemistry, 1969
- A simple chromatographic procedure for the preparation of rabbit-muscle myosin a free from AMP deaminaseBiochimica et Biophysica Acta (BBA) - Protein Structure, 1967
- Studies on the structure of myosinJournal of Molecular Biology, 1962
- THE ENTHALPY CHANGE OF ADENOSINE TRIPHOSPHATE HYDROLYSISJournal of Biological Chemistry, 1956