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. 2010 May 28;192(15):4037–4044. doi: 10.1128/JB.00386-10

FIG. 3.

FIG. 3.

Purification and enzymatic study of Rv0241c. (A) SDS-PAGE analysis of the purification steps. Lane 1, molecular weight markers; lane 2, cleared cell lysate; lanes 3 to 5, Ni Sepharose FF column (flowthrough, wash, and elution of Rv0241c with 250 mM imidazole); lane 6, Superdex 75 gel filtration column (elution fraction containing Rv0241c). Gels (20% polyacrylamide) stained with Coomassie blue are shown. The dividing lines separate different parts of the gel. (B) Chain length specificity profile. (C) Acyl chain carrier specificity. In panels B and C, the specific activities of Rv0241c were measured at fixed concentrations of substrate (2.5 μM) and enzyme (8 nM) in 100 mM sodium phosphate buffer (pH 7.0). The data are means ± the standard deviation.