A transient kinetic study of enthalpy changes during the reaction of myosin subfragment 1 with ATP.
- 15 December 1987
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 248 (3) , 683-690
- https://doi.org/10.1042/bj2480683
Abstract
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 and Gutfreund (1987) Biochem. J. 248, 677-682]. 2. At 5.degree.C and pH 7.0, the endothermic on-enzyme ATP-cleavage step was observed directly (.DELTA.H = +64 kJ .cntdot. 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.This publication has 26 references indexed in Scilit:
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