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Mass spectrometry of 6His-SipB and endogenous SipB purified from S. Typhimurium.

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posted on 2017-01-13, 17:38 authored by Julie P. Viala, Valérie Prima, Rémy Puppo, Rym Agrebi, Mickaël J. Canestrari, Sabrina Lignon, Nicolas Chauvin, Stéphane Méresse, Tâm Mignot, Régine Lebrun, Emmanuelle Bouveret

MALDI-TOF mass spectrometry analysis of intact purified SipB. On the upper left of each graph is indicated the version of the purified SipB protein that has been analyzed by MALDI-TOF mass spectrometry and the organism from which it was purified: Stm for S. Typhimurium. A. The protein 6His-SipB was produced in the S. Typhimurium ΔiacP genetic background from production plasmids co-expressing iacP or not (S2B Fig for production plasmids); B. The intact native SipB was purified from S. Typhimurium WT and ΔiacP (strains JV1 and JV52) using an immunosorbent.

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