What is it about?
The biomolecular processes which translocate toxic metals that have infiltrated the bloodstream to organs ultimately define the exposure-response relationship, but are poorly understood. To gain insight, we have labeled pure HSA with Hg2+ and Cd2+ (molar ratio 1:0.1:01) and analyzed this bis-metallated plasma protein with size exclusion chromatography coupled on-line to an inductively coupled plasma atomic emission spectrometer (SEC-ICP-AES) using PBS-buffer as the mobile phase. The addition of increasing concentrations of L-cysteine (Cys) to this mobile phase allowed to observe the comparative mobilization of these metals. We observed that 50 micromolar Cys in the mobile phase more easily mobilized Hg2+ than Cd2+.
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Why is it important?
Our results suggest that Hg2+ is more easily translocated from blood plasma binding proteins to toxicological target organs than Cd2+ at near physiological conditions thus providing insight into their toxicological chemistry in the bloodstream.
Perspectives
Our chosen liquid chromatography-based approach is amenable to be extended to probe the interaction of other small molecular weight species that are present in human blood plasma with plasma protein bound toxic metal species. This approach has the potential to unravel the biomolecular mechanisms that link exposure to toxic metal species with organ-based adverse health effects in mammals.
Dr Juergen Gailer
University of Calgary
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This page is a summary of: More Effective Mobilization of Hg2+ from Human Serum Albumin Compared to Cd2+ by L-Cysteine at Near-Physiological Conditions, Toxics, July 2023, MDPI AG,
DOI: 10.3390/toxics11070599.
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