Speciation of protein bound trace elements by gel electrophoresis and atomic spectrometry

Ma, Renli, McLeod, Cameron, Tomlinson, Kerry and Poole, Robert (2004) Speciation of protein bound trace elements by gel electrophoresis and atomic spectrometry. Electrophoresis, 25 (15). pp. 2469-2477. ISSN 0173-0835

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Official URL: http://dx.doi.org/10.1002/elps.200405999


The metabolism of trace elements, in particular their binding to proteins in biological systems is of great importance in biochemical, toxicological, and pharmacological studies. As a result there has been a sustained interest over the last two decades in the speciation of protein-bound metals. Various analytical approaches have been employed, combining efficient separation of metalloproteins by liquid chromatography or electrophoresis with high-sensitivity elemental detection. Slab-gel electrophoresis (GE) is a key platform for high-resolution protein separation, and has been combined with autoradiography and various atomic spectrometric techniques for in-gel determination of protein-bound metals. Recently, the combination of GE with state-of-the-art inductively coupled plasma-mass spectrometry (ICP-MS), particularly when linked to laser ablation (LA) for direct gel interrogation, has opened up new opportunities for rapid characterization of metalloproteins. The use of GE and atomic spectrometry for the speciation of protein-bound trace elements is reviewed in this paper. Technical requirements for gel electrophoresis/atomic spectrometric measurement are considered in terms of method compatibilities, detection capability and potential usefulness. The literature is also surveyed to illustrate current status and future trends.

Item Type: Article
Additional Information: Prepared the invited article with Prof. McLeod, which has been cited 19 times since August 2004. It was the very first comprehensive study on metallo-protein characterisation by the gel electrophoresis - atomic spectrometry approach.
Subjects: F300 Physics
Department: Faculties > Health and Life Sciences > Applied Sciences
Depositing User: EPrint Services
Date Deposited: 23 Dec 2008 11:44
Last Modified: 31 Jul 2021 08:38
URI: http://nrl.northumbria.ac.uk/id/eprint/306

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