Sylviane Chevreux et al 2009 J. Phys.: Conf. Ser. 190 012205 doi:10.1088/1742-6596/190/1/012205
Sylviane Chevreux1, Pier Lorenzo Solari2, Stéphane Roudeau1, Guillaume Deves1, Isabelle Alliot3,4, Denis Testemale3,5, Jean Louis Hazemann3,5 and Richard Ortega1
Show affiliationsIsoelectric point isoforms of a metalloprotein, copper-zinc superoxide dismutase (CuZnSOD), separated on electrophoresis gels were analyzed using X-ray Absorption Spectroscopy. Mutations of this protein are involved in familial cases of amyotrophic lateral sclerosis. The toxicity of mutants could be relied to defects in the metallation state. Our purpose is to establish analytical protocols to study metallation state of protein isoforms such as those from CuZnSOD. We previously highlighted differences in the copper oxidation state between CuZnSOD isoforms using XANES. Here, we present the first results for EXAFS analyses performed at Cu and Zn K-edge on the majoritary expressed isoform of human CuZnSOD separated on electrophoresis gels.
Issue 1 (2009)
Sylviane Chevreux et al 2009 J. Phys.: Conf. Ser. 190 012205
Yaguo Lei and Ming J Zuo 2009 Meas. Sci. Technol. 20 125701
Victoria L Mazalova et al 2009 J. Phys.: Conf. Ser. 190 012127
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