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. 2005 May;71(5):2632–2641. doi: 10.1128/AEM.71.5.2632-2641.2005

FIG. 1.

FIG. 1.

SDS-PAGE analysis of purified AhlM. The enzyme was purified from recombinant S. lividans, as described in Materials and Methods. The pooled active fractions were loaded on SDS-12% PAGE after Ni affinity chromatography. The arrowheads indicate the bands corresponding to two subunits of AhlM. Lane M, size marker; lane 1, purified AhlM.