A substoicheiometric assay for the determination of free adenosine triphosphate in the presence of reversibly bound adenosine triphosphate
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چکیده
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Adenosine triphosphate - Wikipedia, the free encyclopedia
Adenosine5'-triphosphate (ATP) is a multifunctional nucleotide used in cells as a coenzyme. It is often called the "molecular unit of currency" of intracellular energy transfer.[1] ATP transports chemical energy within cells for metabolism. It is produced by photophosphorylation and cellular respiration and used by enzymes and structural proteins in many cellular processes, including biosynthet...
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Factors affecting inhibition of myosin ATPase by ATP, such as concentration of the enzyme, of ATP, and of the divalent metals, calcium and magnesium, have been studied and the results are reported here. Experiments were carried out under conditions in which no known magnesium effects occurred, so that only the effect of calcium on the nucleoside triphosphatase activity of myosin A could be qual...
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due to the limiting workspace of parallel manipulator and regarding to finding the trajectory planning of singularity free at workspace is difficult, so finding a best solution that can develop a technique to determine the singularity-free zones in the workspace of parallel manipulators is highly important. in this thesis a simple and new technique are presented to determine the maximal singula...
15 صفحه اولThe 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, ...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1970
ISSN: 0306-3283
DOI: 10.1042/bj1160039pb