Figure 2

SDS-PAGE analysis of the production of rADI. (A) Co-expression with GroES-GroEL chaperones (B) Truncation of the N-terminal 30 amino acids. (C) The combined addition of D-glucose and L-arginine in LB medium. All the protein samples were normalized at OD₆₀₀. In (A), M, molecular-mass marker protein; lanes 1–2: supernatant and cell debris of the pET-30a(+)-harboring E. coli BL21(DE3) cells; lanes 3–4: supernatant and cell debris of pET30a-ADI-harboring E. coli BL21(DE3) alone; lanes 5–6: supernatant and cell debris of pET30a-ADI-harboring E. coli BL21(DE3) cells co-expressed with GroES-GroEL. In (B), lanes 1–2: supernatants of cells harboring rADI and truncated rADI; lanes 3–4: cell debris of cells harboring rADI and truncated rADI. In (C), lanes 1–2: supernatant and cell debris of cells harboring pET30a-ADI and pGro7 from cultures containing 0.5% L-arginine; lanes 3–4: supernatant and cell debris of cells harboring pET30a-ADI and pGro7 from cultures containing 0.5% D-glucose; lanes 5–6: supernatant and cell debris of cells harboring pET-30a(+) and pGro7 from cultures containing 0.5% L-arginine and 0.5% D-glucose; lanes 7–8: supernatant and cell debris of cells harboring pET30a-ADI and pGro7 from cultures containing 0.5% L-arginine and 0.5% D-glucose; lane M: molecular-mass marker protein.