US EPA

5101396 

Journal Article 

Investigations on the binding of ethylmercury from thiomersal to proteins in influenza vaccines 

Strohmidel, P; Sperling, M; Karst, U 

2018 

1 

Journal of Trace Elements in Medicine and Biology
ISSN: 0946-672X
EISSN: 1878-3252 

Elsevier GmbH 

50 

100-104 

English 

30262265 

10.1016/j.jtemb.2018.06.011 

WOS:000448633900013 

https://www.scopus.com/inward/record.uri?eid=2-s2.0-85048732231&doi=10.1016%2fj.jtemb.2018.06.011&partnerID=40&md5=70f635d1925fbe78368d9f41cce95be9
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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. 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+ and a high-molecular compound could be observed for different concentrations of EtHg+ 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+ and a binding of 141 μg L-1 Hg was shown for a vaccine solution that was incubated with EtHg+ (25 mg L-1 Hg). 

Hyphenated techniques; Influenza vaccines; Mercury speciation; SEC/ICP-MS; Thiomersal; TXRF