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. 1987 Dec 15;248(3):683–690. doi: 10.1042/bj2480683

A transient kinetic study of enthalpy changes during the reaction of myosin subfragment 1 with ATP.

N C Millar 1, J V Howarth 1, H Gutfreund 1
PMCID: PMC1148603  PMID: 2829836

Abstract

1. The enthalpy changes during individual reaction steps of the myosin subfragment 1 ATPase were studied with the use of a new stopped-flow calorimeter [Howarth, Millar & Gutfreund (1987) Biochem. J. 248, 677-682]. 2. At 5 degrees C and pH 7.0, the endothermic on-enzyme ATP-cleavage step was observed directly (delta H = +64 kJ.mol-1). 3. ADP binding is accompanied by a biphasic enthalpy change. 4. The release and uptake of protons was investigated by the use of two buffers with widely different heats of ionization. 5. Protons are involved in all four principal steps of the myosin subfragment 1 ATPase.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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