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. 2007 Feb 16;6(4):584–591. doi: 10.1128/EC.00376-06

FIG. 3.

FIG. 3.

(A and B) Sypro ruby staining of SDS-PAGE-resolved protein fractions obtained by tandem affinity purification of protein complexes from transgenic parasites expressing the PfEF-1β-PTP recombinant protein (A) and the wild-type 3D7 parasites (B). About 0.015% (vol/vol) of the total protein extract (TE), 0.5% of the TEV protease eluate (TEV-EL), and 80% of the final EGTA eluate (F-EL) were fractionated on a 12.5% SDS-PAGE gel. All the bands obtained in the F-EL column were excised and submitted for mass spectrometry analysis. (C) Sequence alignment of the polypeptide sequences of EF-1δ from P. falciparum (PfEF-1δ; accession no. NP_473308), Cryptosporidium hominis (ChEF-1δ; accession no. XP_665336), and Arabidopsis thaliana (AtEF-1δ; accession no. NP_174314). Sequence identity is indicated in dark gray, and similarity is indicated in light gray.