tetano
Editor, Senior Moderator
J Trace Elem Med Biol. 2018 Dec;50:100-104. doi: 10.1016/j.jtemb.2018.06.011. Epub 2018 Jun 18.
[h=1]Investigations on the binding of ethylmercury from thiomersal to proteins in influenza vaccines.[/h] Strohmidel P[SUP]1[/SUP], Sperling M[SUP]2[/SUP], Karst U[SUP]3[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] This study investigates the binding of ethylmercury (EtHg[SUP]+[/SUP]) 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[SUP]+[/SUP] 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. First experiments showed the necessity of a rinsing step during elution with a thiol-containing compound to prevent unspecific binding or mercury species to the chromatographic system. Adduct formation of EtHg[SUP]+[/SUP] and a high-molecular compound could be observed for different concentrations of EtHg[SUP]+[/SUP] applied. The mercury-containing fraction was larger than 133 kDa, indicating binding to hemagglutinin, which is the active ingredient in influenza vaccines. The applied SEC/ICP-MS method allowed for external calibration with EtHg[SUP]+[/SUP] and a binding of 141 μg L[SUP]-1[/SUP] Hg was shown for a vaccine solution that was incubated with EtHg[SUP]+[/SUP] (25 mg L[SUP]-1[/SUP] Hg).
[h=4]KEYWORDS:[/h] Hyphenated techniques; Influenza vaccines; Mercury speciation; SEC/ICP-MS; TXRF; Thiomersal
PMID: 30262265 DOI: 10.1016/j.jtemb.2018.06.011
[h=1]Investigations on the binding of ethylmercury from thiomersal to proteins in influenza vaccines.[/h] Strohmidel P[SUP]1[/SUP], Sperling M[SUP]2[/SUP], Karst U[SUP]3[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] This study investigates the binding of ethylmercury (EtHg[SUP]+[/SUP]) 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[SUP]+[/SUP] 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. First experiments showed the necessity of a rinsing step during elution with a thiol-containing compound to prevent unspecific binding or mercury species to the chromatographic system. Adduct formation of EtHg[SUP]+[/SUP] and a high-molecular compound could be observed for different concentrations of EtHg[SUP]+[/SUP] applied. The mercury-containing fraction was larger than 133 kDa, indicating binding to hemagglutinin, which is the active ingredient in influenza vaccines. The applied SEC/ICP-MS method allowed for external calibration with EtHg[SUP]+[/SUP] and a binding of 141 μg L[SUP]-1[/SUP] Hg was shown for a vaccine solution that was incubated with EtHg[SUP]+[/SUP] (25 mg L[SUP]-1[/SUP] Hg).
[h=4]KEYWORDS:[/h] Hyphenated techniques; Influenza vaccines; Mercury speciation; SEC/ICP-MS; TXRF; Thiomersal
PMID: 30262265 DOI: 10.1016/j.jtemb.2018.06.011