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Characterization and a role of Pseudomonas aeruginosa spermidine dehydrogenase in polyamine catabolism, by V. V. Dasu, Y. Nakada, M. Ohnishi-Kameyama, K. Kimura and Y. Itoh

Microbiology vol. 152, part 8, pp. 2265 - 2272

Fig. S1. Resolution of SpdHs purified from P. aeruginosa PAO1 and E. coli BL21(DE3) harbouring plasmid pYI435 (spdH), by SDS-PAGE. lane 1, SpdH (0.2 µg) purified from P. aeruginosa PAO1; lane 2, SpdH (1 µg) purified from E. coli BL21(DE3) harbouring pYI435; lane 3, protein markers: phosphorylase b (97 kDa), bovine serum albumin (66 kDa), ovalbumin (45 kDa), carbonic anhydrase (30 kDa) and catalase (20 kDa). [PDF] (46 kb)

Fig. S2. Consumption of spermidine (A) and spermine (B) by P. aeruginosa PAO1 and PAO4548 (spdH::Gm). Wild-type and spdH mutant cells (1x10⁹ ml^-1) growing exponentially in MMP containing 20 mM spermidine (inducible substrate) or 20 mM glutamate (non-inducible substrate) as sole carbon and nitrogen sources were transferred to fresh MMP containing 20 mM spermidine (A) or 20 mM spermine (B) and shaken at 37 ^oC. Duplicate portions were removed from cultures at the indicated incubation times and amounts of polyamines were determined by HPCL. Open circles, non-induced PAO1; filled circles, induced PAO1; open squares, non-induced PAO4548; filled squares, induced PAO4548. [PDF] (40 kb)

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