
doi: 10.1002/bit.20039
pmid: 15007847
AbstractTo assess the suitability of transgenic peas as a host for protein production from the perspective of ease of recovery, a strain containing recombinant β‐glucuronidase with poly(histidine) tail (GUSH6) was evaluated for solubility of the target protein in relation to native components (proteins, carbohydrates, and phenolics). Recovery of the recombinant GUSH6 from aqueous extracts by immobilized metal affinity chromatography with coupled Co2+ yielded a nearly pure product with IDA (enrichment factor (EF) = 260) or NTA (EF = 200) resin. Single‐step recoveries were also possible by isoelectric precipitation (EF = 4), polyelectrolyte precipitation (EF = 1.5), and anion‐exchange chromatography (EF = 3.1), but enrichment factors were low. © 2004 Wiley Periodicals, Inc.
Seeds, Chemical Fractionation, Hydrogen-Ion Concentration, Plants, Genetically Modified, Protein Engineering, Pisum sativum, Recombinant Proteins, Glucuronidase
Seeds, Chemical Fractionation, Hydrogen-Ion Concentration, Plants, Genetically Modified, Protein Engineering, Pisum sativum, Recombinant Proteins, Glucuronidase
| selected citations These citations are derived from selected sources. This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | 16 | |
| popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network. | Average | |
| influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | Average | |
| impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network. | Top 10% |
