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Figure 1 | BMC Biotechnology

Figure 1

From: Folding machineries displayed on a cation-exchanger for the concerted refolding of cysteine- or proline-rich proteins

Figure 1

Production of folding machineries from recombinant E. coli. (A) SDS-PAGE analysis of the expression of Arg10-tagged folding machineries in E. coli cultures incubated at 37°C for 6 hr and induced by 0.5 mM IPTG. I, insoluble fraction; M, molecular mass marker; S, soluble fraction; T, total cell lysates. (B) MALDI-TOF analysis of folding machineries purified by a simple ion-exchange chromatography. Mass spectra of purified folding machinery proteins: 3 (mini-chaperone and hPPIase) or 1 (DsbA) ionization states that match the molecular mass prediction of each folding machinery protein. The expressed and purified folding machinery proteins are indicated by arrows.

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