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Toxicity of thimerosal in biological systems: Conformational changes in human hemoglobin, decrease of oxygen binding capacity, increase of protein glycation and amyloid's formation.
Int J Biol Macromol
July 2020
Institute of Chemistry and Biotechnology, Federal University of Alagoas (UFAL), Campus A.C. Simões, 57072-900 Maceió, Alagoas, Brazil. Electronic address:
Thimerosal (TH), an organomercurial compound, is used as a preservative in vaccines and cosmetics. Its interaction with human hemoglobin (Hb) was investigated under physiological conditions using biophysical and biological assays, aiming to evaluate hazardous effects. TH interacts spontaneously with Hb (stoichiometry 2:1, ligand-protein), preferably by electrostatic forces, with a binding constant of 1.
View Article and Find Full Text PDFInvestigations on the binding of ethylmercury from thiomersal to proteins in influenza vaccines.
J Trace Elem Med Biol
December 2018
Institute of Inorganic and Analytical Chemistry, University of Münster, Corrensstr. 28/30, 48149 Münster, Germany. Electronic address:
This study investigates the binding of ethylmercury (EtHg) released from the preservative thiomersal by hydrolysis to proteins in influenza vaccines via ultrafiltration and subsequent total reflection x-ray fluorescence (TXRF) analysis as well as size exclusion chromatography (SEC) hyphenated to inductively coupled plasma-mass spectrometry (ICP-MS). Binding of EtHg to the protein fraction was shown by means of ultrafiltration and TXRF in a qualitative matter. SEC/ICP-MS was applied to gain more information about the molecular weight of the bound protein and quantitative information.
View Article and Find Full Text PDFThimerosal changes protein conformation and increase the rate of fibrillation in physiological conditions: Spectroscopic studies using bovine serum albumin (BSA).
Int J Biol Macromol
July 2018
Laboratório de Instrumentação e Desenvolvimento em Química Analítica (LINQA), Instituto de Química e Biotecnologia, Universidade Federal de Alagoas, Maceió, AL 57072-900, Brazil. Electronic address:
The interaction between bovine serum albumin (BSA) and thimerosal (TM), an organomercury compound widely employed as a preservative in vaccines, was investigated simulating physiological conditions and using different spectroscopic techniques. The results, employing molecular fluorescence showed the interaction occurs by static quenching through electrostatic forces (ΔH < 0 and ΔS > 0), spontaneously (ΔG = -4.40 kJ mol) and with a binding constant of 3.
View Article and Find Full Text PDFIn vitro study of thimerosal reactions in human whole blood and plasma surrogate samples.
J Trace Elem Med Biol
April 2014
University of Münster, Institute of Inorganic and Analytical Chemistry, Corrensstr. 30, Münster 48149, Germany; European Virtual Institute for Speciation Analysis, Mendelstr. 11, Münster 48149, Germany. Electronic address:
Because of its bactericidal and fungicidal properties, thimerosal is used as a preservative in drugs and vaccines and is thus deliberately injected into the human body. In aqueous environment, it decomposes into thiosalicylic acid and the ethylmercury cation. This organomercury fragment is a potent neurotoxin and is suspected to have similar toxicity and bioavailability like the methylmercury cation.
View Article and Find Full Text PDFAdduct formation of Thimerosal with human and rat hemoglobin: a study using liquid chromatography coupled to electrospray time-of-flight mass spectrometry (LC/ESI-TOF-MS).
Metallomics
August 2011
University of Münster, Institute of Inorganic and Analytical Chemistry, Corrensstr. 30, 48149 Münster, Germany.
Thimerosal (THI) is used as a preservative in many vaccines throughout the world. Ethylmercury (EtHg(+)), released from THI in aqueous media, has a high affinity to thiol functions of proteins. In blood, hemoglobin is a likely target protein because of its high abundance and its several free thiol functions.
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