Calorimetric studies of the interaction of myosin with ADP.
Open Access
- 1 December 1976
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 251 (23), 7499-7503
- https://doi.org/10.1016/s0021-9258(17)32877-6
Abstract
No abstract availableThis publication has 20 references indexed in Scilit:
- Temperature-dependent transitions of the myosin-product intermediate at 10 °C in the Mn(II)-ATP hydrolysisBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1975
- On the enthalpy of binding of ADP to heavy meromyosinJournal of Supramolecular Structure, 1975
- A kinetic study of the energy storing enzyme-product complex in the hydrolysis of ATP by heavy meromyosinBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1973
- Thermochemistry of Lysozyme‐Inhibitor BindingEuropean Journal of Biochemistry, 1972
- Thermochemistry of the Avidin‐Biotin ReactionEuropean Journal of Biochemistry, 1972
- Calorimetric investigation of inhibitor binding to rabbit muscle aldolaseBiochemistry, 1971
- Thermodynamics of nicotinamide-adenine dinucleotide addition to the glyceraldehyde 3-phosphate dehydrogenases of yeast and of rabbit skeletal muscle. An equilibrium and calorimetric analysis over a range of temperaturesBiochemistry, 1971
- Equilibrium binding of adenosine diphosphate to myosinBiochemistry, 1969
- The binding of ADP to myosinBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1969
- 147. The acid dissociation constant of the protonated form of tri(hydroxymethyl)methylamineJournal of the Chemical Society, 1963