Analysis of Phosphorus, Metals and Metalloids Bonded to Proteins

3 Analysis of Phosphorus, Metals and Metalloids Bonded to Proteins 

It is well known that a great variety of biomolecules exist where metals and metalloids are bound to proteins and peptides, coordinated by nucleic acids or complexed by polysaccharides and small organic ligands such as organic acids.55 Most proteins contain amino acids with covalently bonded heteroelements such as sulphur, selenium, phosphorus or iodine.51 Several reviews have been published on the development of mass spectrometric techniques for bioanalysis in metal-lomics , which integrate work on metalloproteins, metalloenzymes and other metal containing biomolecules.1 51 53 54 56-59 The authors consider trace metals, metalloids, P and S (so-called 

The complementary use of LC-ESI-ToF-MS and hyphenated ICP-MS with dynamic reaction cell (DRC) for the characterization of native and recombinant copper proteins (of molar mass range 10-20kDa) has been investigated by Hann et al.67 Size exclusion chromatography (SEC) and ion chromatography (IC) were implemented as separation techniques for hyphenated ICP-MS of intact Cu containing proteins. 

The contribution of mass spectrometry to the biosciences, especially in proteomics (the determination of the protein constituents of a cell or organism) of individual components and the quantitative definition of cellular processes, was reviewed by Gaskell.68 

By combining denaturing gel electrophoresis (SDS-PAGE) and LA-ICP-MS an analytical technique was developed for the speciation of selenoproteins in Se contaminated wildlife (waterfowl embryo and fish ovary collected from Se contaminated sites in Wyoming and the San Joaquin Valleys, CA, respectively).72 Polatajko et al. reported on the state of the art of selenium speciation in biological samples.73 

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