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. 1998 May;180(9):2502–2506. doi: 10.1128/jb.180.9.2502-2506.1998

FIG. 1.

FIG. 1

SDS–15% PAGE of 2-aminomuconate deaminase. Purified 2-aminomuconate deaminase (lane 2; 2 μg) was compared with the crude extract (lane 7; 40 μg), the DEAE fraction (lane 6; 20 μg), the Cu(II)-chelating fraction (lane 5; 20 μg), the gel filtration fraction (lane 4; 20 μg), the Hitrap-Q fraction (lane 3; 7 μg), and protein molecular mass standards (lane 1).