EC Number   |
Reference |
|---|
    1.13.11.20 | recombinant thioredoxin-His6-tagged enzyme by affinity chromatography |
724396 |
| 1.13.11.20 | recombinnat enzyme from Escherichia coli strain BL21(DE3) with cleavage of the Thx-His6 tag |
724430 |
| 1.13.11.20 | standard glutathione S-transferase fusion protein purification protocol, gel-filtration chromatography after removing the glutathione S-transferase tag |
674873 |
| 1.13.11.20 | the fusion protein is purified by immobilized metal (Ni2+) affinity chromatography. The liberated enzyme is separated from the His-8-maltose binding protein by immobilized metal affinity chromatography, further purified by gel filtration chromatography, and concentrated. EDTA is obmitted from the buffers used to purifiy enzyme for catalytic studies, and the gel filtration is not used. |
676850 |
| 1.13.11.20 | using acetone fractionation, column chromatography on DEAE-cellulose, Sephadex G-100, hydroxylapatite, DEAE-Sephadex A-25 and Sephadex G-75 |
439542 |
| 1.13.11.20 | using acetone precipitation, first chromatography on DEAE-cellulose column, second chromatography on DEAE-cellulose column, chromatography on Sephadex G-100 column, hydroxyapatite column, DEAE-Sephadex A-25 column and Sephadex G-75 column |
439548 |
| 1.13.11.20 | using acid treatment, ammonium sulfate fractionation and column chromatography with DEAE-cellulose. The purified enzyme is composed of two distinct proteins, it appears that one of them is a catalytic protein named protein-B having tightly bound iron as a prosthetic group, while the other is either a modifier or activating protein named protein-A. Protein-B is found to exist in both an active and an inactive form |
439547 |
| 1.13.11.20 | using filtration, centrifugation, column chromatography on DEAE-cellulose, Sephadex G-50 and cysteine-Sepharose |
439543 |
| 1.13.11.20 | using heat treatment, ammonium sulfate fractionation and column chromatography on DEAE-cellulose, Sephadex G-200 and Sephadex G-100 |
439546 |
