Some pitfalls in PAGE-LA-ICP-MS for quantitative elemental speciation of dissolved organic matter and metalomics

Anal Bioanal Chem. 2009 Jan;393(2):699-707. doi: 10.1007/s00216-008-2384-2. Epub 2008 Oct 16.

Abstract

An experimental approach to evaluate the capabilities and limitations of polyacrylamide gel electrophoresis (PAGE) and laser ablation inductively coupled plasma mass spectrometry (LA-ICP-MS) for quantitative elemental speciation is presented. Two metalloproteins (superoxide dismutase, containing Cu and Zn, and thyroglobulin, containing I) with high binding affinity for metals, and metal-dissolved organic matter (DOM) complexes (from a compost leachate sample) which show different types of metal binding are studied. Iodine can be quantitatively detected in thyroglobulin after PAGE-LA-ICP-MS using either sodium dodecyl sulfate (SDS) PAGE or native PAGE. However, detection of Cu and Zn in superoxide dismutase after PAGE-LA-ICP-MS depends on the conditions of the PAGE method because possible metal losses can occur (either with SDS-PAGE or with native PAGE). The use of PAGE-LA-ICP-MS to study the contribution of DOM to the mobilization of metals from environmental samples is possible, but it depends also on the PAGE separation conditions owing to disequilibrium effects of metal-DOM complexes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Copper / analysis
  • Copper / metabolism
  • Electrophoresis, Polyacrylamide Gel*
  • Hydrocarbons, Iodinated / analysis
  • Hydrocarbons, Iodinated / metabolism
  • Metalloproteins / analysis*
  • Metalloproteins / metabolism*
  • Sensitivity and Specificity
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization*
  • Thyroglobulin / analysis*
  • Thyroglobulin / metabolism
  • Zinc / analysis
  • Zinc / metabolism

Substances

  • Hydrocarbons, Iodinated
  • Metalloproteins
  • Copper
  • Thyroglobulin
  • Zinc