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Contribution of hyphenated CE-ICP/MS in metal/protein interactions studies
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J. Chamoun
Published/Copyright:
December 17, 2007
Summary
By introducing a preliminary in-capillary preconcentration step, CE-ICP/MS was applied to trace metal speciation in proteins. Emphasis was put on metal/protein interactions where CE-ICP/MS is demonstrated to provide informations concerning metal binding and metal exchanges occuring in proteins. Preliminary studies on the fate of several metals in the presence of a mixture of standard proteins were performed. Cadmium was shown to bind mainly to albumin and ceruloplasmin. Cobalt and nickel were detected only in carbonic anhydrase and ceruloplasmin in the mixture of proteins but also in albumin when injected alone.
Received: 2005-1-3
Accepted: 2005-7-4
Published Online: 2007-12-17
Published in Print: 2005-11-1
© Oldenbourg Wissenschaftsverlag, München
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Articles in the same Issue
- Preface: Chemical Speciation
- Transport methods as complementary tools for speciation purposes
- Contribution of hyphenated CE-ICP/MS in metal/protein interactions studies
- Interfacing capillary electrophoresis with inductively coupled plasma mass spectrometry for redox speciation of plutonium
- Preliminary speciation study of Co(II)-citrate system by ion pairing-reversed phase chromatography coupled to UV detector
- Resistance, accumulation and transformation of selenium by the cyanobacterium Synechocystis sp. PCC 6803 after exposure to inorganic SeVI or SeIV
- Uranium(VI) complexation in cell culture medium: influence of speciation on Normal Rat Kidney (NRK-52E) cell accumulation
- Actinide uptake by transferrin and ferritin metalloproteins
- Plutonium speciation affected by environmental bacteria
- Influence of thermodynamic database on the modelisation of americium(III) speciation in a simulated biological medium
- The OECD/NEA TDB review of selected organic ligands
