1 edition of Application of firefly luciferase assay for adenosine triphosphate (ATP) to antimicrobial drug sensitivity testing found in the catalog.
Application of firefly luciferase assay for adenosine triphosphate (ATP) to antimicrobial drug sensitivity testing
by National Aeronautics and Space Administration, for sale by the National Technical Information Service in Washington, Springfield, Va
Written in English
|Statement||H. Vellend ... [et al.].|
|Contributions||Vellend, H., United States. National Aeronautics and Space Administration.|
|The Physical Object|
|Pagination||160 p. in various pagings :|
|Number of Pages||160|
Firefly luciferase covers a wide range of applications. One common usage of the bioluminescence assay is the measurement of intracellular concentration of adenosine triphosphate Cited by: 6. Application. activity assay (30) affinity binding assay (2) affinity chromatography (1) Adenosine 5′-triphosphate (ATP) assay mix. A highly sensitive firefly luciferase cell based assay for quantifying ATP in cell cultures used to measure cell viability.
Firefly luciferase ATP assay development for monitoring bacterial concentrations in water supplies. Cincinnati, OH: U.S. Environmental Protection Agency, Municipal Environmental Research Laboratory: Center for Environmental Research Information [distributor], (OCoLC) Material Type. A selective method for distinguishing bacterial and nonbacterial adenosine triphosphate (ATP) in clinical bacteriological specimens was studied. The method involved incubation of samples with the detergent Triton X and the ATP-hydrolyzing enzyme apyrase. The incubation selectively destroyed ATP in suspensions of various human cells while not affecting the ATP content in microbial Cited by:
Method. ATP is a molecule found in and around living cells, and as such it gives a direct measure of biological concentration and is quantified by measuring the light produced through its reaction with the naturally occurring firefly enzyme luciferase using a amount of light produced is directly proportional to the amount of ATP present in the sample. Shining™ Luciferase are perfectly suitable for assays both with native D-luciferin (dLuc) or synthetic pro-luciferins (caged luciferins) 3. Improved applicability for routine luciferin-luciferase tests. A. ATP assays Adenosine triphosphate (ATP) is pr esent in all living cells .
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With the interpretation of results. Both the incubation procedure and the ATP assays are com-patible with automation. Key Woids (Selected by Audioes)) Adenosine triphosphate, firefly luciferase ATP assay, antimicrobial susceptibility testing, antibiotics, urinary tract infections, bacteria Security Clossif.
(of this report) Unclassified Application of firefly luciferase assay for adenosine triphosphate (ATP) to antimicrobial drug sensitivity testing. Washington: National Aeronautics and Space Administration ; Springfield, Va.: For sale by the National Technical Information Service, (OCoLC) Material Type: Government publication, National government publication.
AMP is converted to adenosine triphosphate and coupled to firefly luciferase. With this procedure, kinetic parameters (K m, k cat) for SAHH were obtained, in good agreement with literature values. Assay characteristics include sustained light output combined with ultrasensitive detection (10 –7 unit of SAHH).
The assay is documented with the characterization of slow-onset inhibition for Cited by: AMP is converted to adenosine triphosphate and coupled to firefly luciferase. With this procedure, kinetic parameters (Km, kcat) for SAHH were obtained, in good agreement with literature values.
Assay characteristics include sustained light output combined with ultrasensitive detection (10–7 unit of SAHH).Cited by: Key words: Firefly luciferase, ATP, cells, McCoy CT A method for determining intracellular content of adenosine triphosphate (ATP) in the cultured cells was investigated with a firefly luciferase reagent, and a micro assay method was established.
The method minimized the size of both samples and luciferase reagent employed. The firefly luciferase-based assay differs from most familiar enzyme-based determinations.
Most enzyme assays are based either on the production of a product or the disappearance of a substrate. Usually the compound measured is stable so that its concentration can be determined after a Cited by: A rapid (15 min) test for bacteriuria based on firefly luciferase analysis of bacterial ATP has been evaluated in 2, clinical urine specimens.
The test procedure involves removal of nonbacterial ATP by treatment of urine with Triton X and apyrase, extraction of bacterial ATP by boiling, and bioluminescent analysis of bacterial ATP by Cited by: Use of firefly luciferase to assay adenosine triphosphate (ATP) extracted from microorganisms provides an easy means to enumerate microbes within minutes.
The small amount of light produced is proportional to ATP and thus microbial number. The average bacterium contains around 10 Cited by: The luminescence of PTD-conjugated firefly luciferase should prove advantageous for many in vivo applications involving pharmaceuticals.
Here, we evaluated the applicability of PTD-Luc as an ATP sensor for measuring the intracellular ATP content. The greatest advantage of PTD-Luc is that it allows the rapid, Cited by: Theoretical aspects of the adenosine triphosphate bioluminescence assay based on the use of the firefly luciferin–luciferase system are considered, as well as its application for assessing cell viability in microbiology, sanitation, medicine, and ecology.
Various approaches for the analysis of individual or mixed cultures of microorganisms are presented, and capabilities of the method for Cited by: Request PDF | Luciferase-Based Assay for Adenosine: Application to S-Adenosyl-L-homocysteine Hydrolase | S-Adenosyl-L-homocysteine hydrolase (SAHH) catalyzes the reversible conversion of S.
boiling buffer and assayed by the firefly luciferase assay. Application of the. method to clinical urine specimens showed that the ATP level after. treatment with Triton/apyrase was correlated to bacterial counts and that the.
sensitivity of the assay was sufficient for the detection of bacteria/ml. Luciferase preparations are available commercially. The quantitative determination of ATP and creatine phosphate is described here. Assay methods for related substrates (e.g. mixtures of ATP, ADP, AMP and creatine phosphate) and enzymes (myokinase, hexokinase, apyrase, creatine kinase) can be found in the original papers of Strehler and Totter Cited by: Detection of bacteriuria by luciferase assay of adenosine triphosphate.
A Thore, ATP remaining in the sample after incubation was extracted in boiling buffer and assayed by the firefly luciferase assay. Application of the method to clinical urine specimens showed that the ATP level after treatment with Triton/apyrase was correlated to.
USA US07/, USA USA US A US A US A US A US A US A US A US A US A Authority US United States Prior art keywords luciferase mm coa luciferin concentration Prior art date Legal status (The legal status is an assumption and is not a legal by: Ignowski, J.M. & Schaffer, D.V. Kinetic analysis and modeling of firefly luciferase as a quantitative reporter gene in live mammalian cells.
Biotechnol. Bioeng. 86, – ().Cited by: AMP is converted to adenosine triphosphate and coupled to firefly luciferase. With this procedure, kinetic parameters (K m, k cat) for SAHH were obtained, in good agreement with literature values.
Assay characteristics include sustained light output combined with ultrasensitive detection (10 -7 unit of SAHH).Cited by: have used the firefly luciferin-luciferase assay, which measures ATP directly, to study herbicide effects on phosphorylation processes in vivo.
A detailed study of our method, as well as the use of the Arninco Chem-Glow Photom- eter,* has been published elsewhere (St. BioThema is entirely focused on analytical applications of the firefly luciferase reaction.
This reaction can be used for assays of number of cells, cell proliferation and cytotoxicity, all enzymes and metabolites participating in ATP forming or degrading reactions, reporter gene assays.
S-Adenosyl-L-homocysteine hydrolase (SAHH) is the sole enzyme responsible for the catabolism of S-adenosyl-L-homocysteine (SAH) in mammals; it catalyzes the hydrolysis of SAH to adenosine (ADO) and L-homocysteine (Hcy). 1 Although the reaction is reversible in vitro, the occurrence of adenosine kinase (AK) and adenosine deaminase (ADA) in cells shifts the chemical.
Bioluminescence-based methods for the detection of bacteria can be divided into two: adenosine triphosphate (ATP) measurement, and lux gene technology. Extraction and measurement of bacterial ATP can be indicative of the number of organisms present in a sample.
The firefly luciferin –luciferase system is the most commonly used method. In the presence of ATP, the enzyme luciferase causes .ENLITEN® ATP Assay System Bioluminescence Detection Kit for ATP Measurement 1.
Description The ENLITEN® ATP Assay System is intended for the rapid and quantitative detection of adenosine 5´-triphosphate (ATP). The rL/L Reagent included in the system is .TEST METHOD FOR ATP SENSITIVITY OF LUCIFERASE. If necessary, follow steps and to set and standardize the Luminometer.
Prepare reaction cocktail by adding mL of reagent (ATP2) to mL of reagent (Firefly). Pipette (in milliliters) the following reagents into suitable test tubes.