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. 2003 Aug;69(8):4390–4395. doi: 10.1128/AEM.69.8.4390-4395.2003

FIG. 1.

FIG. 1.

Purification of nitroreductases fused to GST. E. coli DH5α (pGST-EcNfsA), E. coli DH5α (pGST-EcNfsB), and E. coli DH5α (pGST-VhNfsA) were cultured to exponential phase in LB broth and then induced by the addition of 0.5 mM IPTG for 3.5 h. Induced cells were broken by sonication and separated into supernatant and pellet fractions by centrifugation. By using affinity chromatography of glutathione and GST, GST-EcNfsA, GST-EcNfsB, and GST-VhNfsA (lanes 3, 4, and 5, respectively) were purified. Lanes 2 and 6 show GST (26 kDa) and BSA (66 kDa), respectively. Lane 1 has molecular-mass standards.