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2000
Volume 20, Issue 2
  • ISSN: 1570-1646
  • E-ISSN: 1875-6247

Abstract

Background: Ricin is the most toxic protein known. It is part of the ribosome-inactivating proteins, RIPs, type 2, which has generated importance in his research; it is possible to detoxify this protein with phenolic compounds; however, it is essential to understand how this detoxification occurs. To analyze using electrophoresis, UV-visible spectroscopy, and high-performance liquid chromatography (HPLC) the protein ricin with the flavonol quercetin, understanding the detoxification process.Methods: The UV-visible analysis was performed on both the supernatant and the precipitate of the samples; these results were analyzed using one-factor analysis of variance (ANOVA) and a Tukey test with a significance level of 0.05.Results: 34.9 μg/mL of total protein and 4.2 μg / mL of ricin were obtained in the extraction method. Eight interactions were carried out, and all presented precipitation, observing through the electrophoresis technique a decrease in the bands corresponding to the protein; these results were analyzed with HPLC observing a decrease in the size of the area of the peaks in the chromatograms.Conclusion: The results obtained in this study suggest an agglomeration of the protein, generating a precipitate that could benefit the protein's inactivation as a detoxification process.

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/content/journals/cp/10.2174/1570164620666230717114018
2023-04-01
2025-09-05
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/content/journals/cp/10.2174/1570164620666230717114018
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  • Article Type:
    Research Article
Keyword(s): electrophoresis; HPLC; interaction; quercetin; Ricin; UV-Vis
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