EC Number   |
|---|
   3.4.22.10 | - |
| 3.4.22.10 | a combination of two successive strong cation exchange resins gives the best results for soluble, pure enzyme with the highest activity |
| 3.4.22.10 | HiTrap SP column chromatography, and G75 Sephadex gel filtration |
| 3.4.22.10 | native mature Spe B by ammonium sulfate fractionation, dialysis, and ion exchange chromatography, recombinant His-tagged Spe B propeptide and SpeB mutant C47S from Escherichia coli |
| 3.4.22.10 | Ni2+-chelating column chromatography |
| 3.4.22.10 | recombinant His-tagged wild-type and mutant C192S enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, the wild-type enzyme autoprocesses during purification to the mature 28 kDa protein |
| 3.4.22.10 | recombinant pro-sequence domain and refolded mature enzyme from Escherichia coli by affinity chromatography |
| 3.4.22.10 | recombinant wild-type and inactive mutant enzyme from Escherichia coli by affinity chromatography |
| 3.4.22.10 | the proteins are purified by Ni2+-chelating chromatography with a gradient of 20-200 mM imidazole. The proteins are concentrated by ultrafiltration using a 10 kDa cutoff membrane and then exchanged with phosphate-buffered saline |
| 3.4.22.10 | using Ni-NTA chromatography |
