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Issue 5, 2009
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Methylmercury speciation in fish muscle by HPLC-ICP-MS following enzymatic hydrolysis

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Abstract

Monomethylmercury (MeHg+ and its complexes; hereafter referred to as MeHg) in the intracellular environment is known to be predominantly bonded to thiol-containing biomolecules, but the actual identities of these target biomolecules remain unknown. While binding with glutathione acts as a detoxification mechanism for MeHg, binding with L-cysteine is thought to be the main pathway of MeHg transport across the blood–brain barrier. Here we report a HPLC-ICP-MS method that is capable of separating and analyzing MeHg-cysteine complexes (MeHgCys; charges are neglected for simplicity) and MeHg-glutathione complexes (MeHgGlu), as well as MeHgX (X = H2O, OH, or Cl) and inorganic HgX, with detection limits at the sub-micromolar levels. The method was successfully applied for the determination of MeHg speciation in a dogfish muscle sample after enzymatic hydrolysis with trypsin, and provided the first analytical evidence for the presence and dominance of MeHgCys in fish muscle.

Graphical abstract: Methylmercury speciation in fish muscle by HPLC-ICP-MS following enzymatic hydrolysis

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Publication details

The article was received on 07 Nov 2008, accepted on 19 Jan 2009 and first published on 18 Feb 2009


Article type: Paper
DOI: 10.1039/B819957B
Citation: J. Anal. At. Spectrom., 2009,24, 663-668
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    Methylmercury speciation in fish muscle by HPLC-ICP-MS following enzymatic hydrolysis

    M. Lemes and F. Wang, J. Anal. At. Spectrom., 2009, 24, 663
    DOI: 10.1039/B819957B

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