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. 1999 Mar;181(5):1444–1450. doi: 10.1128/jb.181.5.1444-1450.1999

FIG. 2.

FIG. 2

SDS-PAGE analysis during purification of the 3HAP mutase from R. eutropha JMP134. Lanes 3 and 8 contained the following molecular mass standards (from top to bottom): bovine serum albumin (67 kDa), ovalbumin (43 kDa), carbonic anhydrase (30 kDa), and soybean trypsin inhibitor (20 kDa). All other lanes contained 0.5 μg of protein from the respective preparations of the mutase. Lane 1, cell extract after ultracentrifugation; lane 2, pooled fractions from DEAE anion-exchange chromatography; lanes 4, 6, and 7, pooled fractions from butyl agarose hydrophobic interaction chromatography, each containing 3HAP mutase with minor contaminations; lane 5, pooled fraction from butyl agarose hydrophobic interaction chromatography containing purified 3HAP mutase.