Research Article

Molecular Characterization of a Recombinant Manganese Superoxide Dismutase from Lactococcus lactis M4

Figure 3

SDS-PAGE analysis of the pooled fractions after each purification step. SDS-PAGE was performed on 12% denatured polyacrylamide gel. (a) SDS-PAGE analysis of pooled fractions with SOD activity after IMAC: M, protein molecular weight marker (Fermentas); lane 1, pooled peak 1 (6 μg); lane 2, pooled peak 2 (6 μg); (b) SDS-PAGE analysis of pooled fractions after gel filtration: M, protein molecular weight marker (Fermentas); lane 1, crude extract (10 μg); lane 2: pooled SOD active fractions (peak 2) after IMAC (4 μg); lane 3: pooled SOD active fractions after gel filtration chromatography (2 μg); lane 4: dialyzed pooled SOD active fractions after gel filtration chromatography (2 μg); (c) SOD activity staining of the purified native SOD electrophoresed on 10% nondenatured polyacrylamide gel. Lane 1: IMAC; (2) gel filtration; (3) dialyzed sample. The achromatic zone against the purple background revealed the activity of SOD. Each lane is loaded with 2 μg of protein.
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469298.fig.003b
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469298.fig.003c
(c)