THE ENTHALPY CHANGE OF ADENOSINE TRIPHOSPHATE HYDROLYSIS
نویسندگان
چکیده
منابع مشابه
The Enthalpy Change on Adenosine Triphosphate
The energetics of ATP’ hydrolysis to ADP and P have been studied previously by combining either thermal (1, 2) or free energy (3-6) data for a number of chemical reactions according to the usual procedures of chemical thermodynamics. Such calculations, however, suffer from the fact that the uncertainties in each measurement are compounded in the final result. The ATPase properties of myosin off...
متن کاملThe Eq+librium Constants of the Adenosine Triphosphate Hydrolysis and the Adenosine Triphosphate- Citrate Lyase Reactions
The observed standard free energy change (AGibs) for the hydrolysis of the terminal pyrophosphate bond of ATP has been experimentally determined under physiological conditions using an entirely new set of reactions. The observed equilibrium constant (K,,bs) for the combined reactions of acetate kinase (EC 2.7.2.1) and phosphate acetyltransferase (EC 2.3.1.8) has been determined at 38”, pH 7.0, ...
متن کاملThe equilibrium constants of the adenosine triphosphate hydrolysis and the adenosine triphosphate-citrate lyase reactions.
The observed standard free energy change (AGibs) for the hydrolysis of the terminal pyrophosphate bond of ATP has been experimentally determined under physiological conditions using an entirely new set of reactions. The observed equilibrium constant (K,,bs) for the combined reactions of acetate kinase (EC 2.7.2.1) and phosphate acetyltransferase (EC 2.3.1.8) has been determined at 38”, pH 7.0, ...
متن کاملMechanism of adenosine triphosphate hydrolysis by actomyosin.
The hydrolysis of ATP by acto-HMM has been studied during the transient state using a rapid-mixing apparatus. The rate of substrate binding was slightly slower and the rate of hydrolysis of the first molecule of ATP was essentially the same as for heavy meromyosin (HMM) alone. The rate of acto-HMM dissociation after binding substrate was too fast to measure in a stopped-flow apparatus, conseque...
متن کاملStudies on the Hydrolysis of Adenosine Triphosphate by Spinach Chloroplasts.
During studies on photophosphorylation in cell-free preparations of the blue-green alga, Anabaena variabilis, a photohydrolysis of ATP was found to be induced by high concentrations of cysteine or GSH, while photophosphorylation became inhibited (1, 2). A similar photohydrolysis was also reported with chloroplasts from spinach leaves, but still higher sulfhydryl concentrations were required to ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1956
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)65857-0