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. 2004 Jan 22;32(2):465–476. doi: 10.1093/nar/gkh191

Figure 7.

Figure 7

Estimation of the apparent molecular mass of the purified WT P.abyssi TrmI protein (A) and of the C196S (B), C233S (C) and C196S+C233S (D) mutants by gel filtration chromatography on a Superdex 200 prep grade 16/60 column (Pharmacia Biotech). The samples consisted of 2.5 mg of purified WT or mutant TrmI proteins in 50 mM Tris–HCl pH 8.5, 500 mM KCl, 200 mM imidazole. Elution was performed with the same buffer. The molecular masses of the proteins were calculated using a standard consisting of carbonic anhydrase from bovine erythrocytes (29 kDa), bovine serum albumin (66 kDa), bovine serum albumin dimer (132 kDa) and β-amylase from sweet potato (200 kDa).