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FEBS Lett. 1997 Aug 25;413(3):473-6.

Electrospray ionization mass spectrometry analysis of the apo- and metal-substituted forms of the Fur protein.

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Département de Recherche Fondamentale sur la Matière Condensée, (Unité de Recherche Associée au CNRS No. 1194), CEA-Grenoble, France.


Fur has been purified and reconstituted with Co2+ and Mn2+. The ESI-MS spectra of the apoprotein as well as Mn-Fur and Co-Fur under acidic denaturating conditions showed the existence of two species of molecular mass 16,660 +/- 3 and 16,792 +/- 3 Da, which correspond, respectively, to the N-terminal methionine 'excised' or 'non-excised' forms of the monomer. This result proves the absence of any other post-translational modification or modification due to metal incorporation. On the other hand, under soft conditions, ESI spectra provided for the first time direct evidence for dimeric metal-containing forms in solution.

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