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ATP is quantified by measuring the light produced through its reaction with the naturally occurring firefly enzyme luciferase using a luminometer. The amount of light produced is directly proportional to the amount of ATP present in the sample. ATP tests can be used to: Control biological treatment reactors; Guide biocide dosing programs
An ATP test is the process of rapidly measuring active microorganisms in water through detection adenosine triphosphate (ATP). ATP is a molecule found only in and around living cells, and as such it gives a direct measure of biological concentration and health.
ATP:ATP is a common energy molecule that many researchers hold extensive knowledge of, thus carrying over to how one understands viability assays. The ATP Assay Concept is a well-known technique for determining the viability of cells using the assessment of ATP and a method known as "firefly luciferase". [5]
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TNP-ATP is a fluorescent molecule that is able to determine whether a protein binds to ATP, and the constants associated with that binding.It is primarily used in fluorescence spectroscopy, but is also very useful as an acceptor molecule in FRET, and as a fluorescent probe in fluorescence microscopy and X-ray crystallography.
Cells detect ATP using the purinergic receptor proteins P2X and P2Y. [40] ATP has been shown to be a critically important signalling molecule for microglia - neuron interactions in the adult brain, [41] as well as during brain development. [42] Furthermore, tissue-injury induced ATP-signalling is a major factor in rapid microglial phenotype ...
Ohio Agricultural Research and Development Center (OARDC) is the research institution of the Ohio State University College of Food, Agricultural, and Environmental Sciences. The center is home to research projects ranging from plant and animal sciences to human ecology and medicine, and includes branches across the state covering a total of ...
The structure of the intact ATP synthase is currently known at low-resolution from electron cryo-microscopy (cryo-EM) studies of the complex. The cryo-EM model of ATP synthase suggests that the peripheral stalk is a flexible structure that wraps around the complex as it joins F 1 to F O.