TABLE 1.
Purification of PCMH from G. metallireducens
| Purification step | Total protein (mg) | Enzymatic activityb
|
Yield of recovery (%) | Purification (fold) | |
|---|---|---|---|---|---|
| Total (nmol min−1) | Specific (nmol min−1 mg−1) | ||||
| Crude extracta | 819 | 4,750 | 5.8 | 100 | 1 |
| Washed membrane | 88 | 1,473 | 16.7 | 31 | 2.9 |
| LDAO-treated membrane | 66.2 | 417 | 6.3 | 9 | 1.1 |
| NaCl supernatant | 46.9 | 1,186 | 25.3 | 25 | 4.4 |
| Gel filtration pool | 9.6 | 988 | 103 | 21 | 17.8 |
| Octyl Sepharose pool | 0.4 | 880 | 2,200 | 18 | 380 |
a
Crude extract was from 12 g of G. metallireducens cells grown on p-cresol with Fe(III) as the electron acceptor.
b
Enzymatic activities were determined with the HPLC assay in crude extract and membrane fractions and with the spectrophotometric assay in soluble fractions.