ArticleAnalytical biochemistry2002
A novel fluorescence competitive assay for glucose determinations by using a thermostable glucokinase from the thermophilic microorganism Bacillus stearothermophilus.
Article in Analytical biochemistry, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed, 45 citations in OpenAlex.
- Review
- Addressing the Selectivity of Enzyme Biosensors: Solutions and Perspectives.Sensors (Basel, Switzerland) · 2021Review
- Structure-based design of robust glucose biosensors using a Thermotoga maritima periplasmic glucose-binding protein.Protein science : a publication of the Protein Society · 2007Article
- Proteins from extremophiles as stable tools for advanced biotechnological applications of high social interest.Journal of the Royal Society, Interface · 2007Review
- Microscale enzymatic optical biosensors using mass transport limiting nanofilms. 1. Fabrication and characterization using glucose as a model analyte.Analytical chemistry · 2007Article
- Protein-based biosensors for diabetic patients.Journal of fluorescence · 2004Article
- Fluorescence glucose detection: advances toward the ideal in vivo biosensor.Journal of fluorescence · 2004Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
We describe the use of a thermostable glucokinase in a novel competitive fluorescence assay for glucose. Glucokinase from Bacillus stearothermophilus (BSGK) was found to retain enzymatic activity in solution for over 20 days. The single cysteine residue in BSGK, which is near the active site, was labeled with a fluorescent probe, 2-(4-iodoacetamidoanilino)naphthalene-6-sulfonic acid. The ANS-labeled BSGK displayed a modest 25% decrease in the emission intensity upon binding glucose but no change in lifetime. To obtain a larger spectral change we developed a competitive assay for glucose using the intrinsic tryptophan fluorescence from BSGK and a resonance energy transfer (RET) acceptor-labeled sugar. The sugar-labeled acceptor quenched the BSGK tryptophan emission, and the quenching was reversed upon addition of glucose. The use of RET as the sensing mechanism can be easily extended to longer wavelengths for a more practical glucose sensor.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.