ArticleJournal of fluorescence2014
Fluorescence interaction and determination of sulfathiazole with trypsin.
Article in Journal of fluorescence, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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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Who cites it
1 citing paper in PubMed, 24 citations in OpenAlex.
- Study of Binding Properties Between Two New Ibuprofen and Naproxen Based Acyl Hydrazone Derivatives and Trypsin.Journal of fluorescence · 2016Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The mechanism of interaction of trypsin with the sulfathiazole was studied through using fluorescence quenching and UV-visible absorption spectra at pH 7.4. The Stern-Volmer quenching constants, binding constants, number of binding sites and the corresponding thermodynamic parameters ΔH(o), ΔS(o) and ΔG(o) were calculated at different temperatures. The effect of common metal ions on the constants was also discussed. The results suggest that sulfathiazole can interact strongly trypsin and that there is the formation of trypsin-sulfathiazole complex and the interaction can be explained on the basis of hydrogen bonds and van der Waals forces. The binding distance (r) between the donor (trypsin) and acceptor (sulfathiazole) was 3.52 nm based on the Förster's non-radiative energy transfer theory. The detection and quantification limits of sulfathiazole were calculated as 2.52 and 8.40 μM in the presence of trypsin, respectively. The relative standard deviation (RSD) was 4.086% for determinations (n = 7) of a sulfathiazole solution with the concentration of 7.54 μM.
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Registered trials
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