Author(s): Yun Z, Li L, Liu L, He B, Zhao X,
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Abstract Characterization of mercury binding protein in the human body is very important for understanding the metabolism and the mechanism of toxication of ingested mercuric compounds. In this study, mercury-containing protein in human plasma was separated by on-line heart-cutting two-dimensional high performance liquid chromatography (2D-HPLC). This 2D separation system used size exclusion liquid chromatography (SEC) followed by weak anion exchange liquid chromatography (WAX) and the two LC parts were coupled by a six-port valve equipped with a storage loop and controled by the computer. The WAX effluent was determined by both UV detection and inductively coupled plasma-mass spectrometry (ICP-MS) to locate the mercury-containing protein. A unique mercury-containing protein fraction was obtained by 2D-HPLC separation and subsequently identified by HPLC coupled with linear ion trap-Fourier transform ion cyclotron resonance mass spectrometry (HPLC-LTQ-FT). The database search confirmed that the mercury-containing protein in the human plasma is human serum albumin (HSA). The stoichiometry and thermodyamics interaction of inorganic mercury (Hg(2+)) with HSA was studied by isothermal titration calorimetry (ITC) and two binding types were observed. Mercury-containing protein in human plasma was separated and identified in the present study and it is important for understanding the metabolism of mercury in the human body.
This article was published in Metallomics
and referenced in Journal of Analytical & Bioanalytical Techniques