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Recombinant protein purification from pea.
- Source :
-
Biotechnology and bioengineering [Biotechnol Bioeng] 2004 Apr 05; Vol. 86 (1), pp. 108-14. - Publication Year :
- 2004
-
Abstract
- To assess the suitability of transgenic peas as a host for protein production from the perspective of ease of recovery, a strain containing recombinant beta-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 Co(2+) 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.<br /> (Copyright 2004 Wiley Periodicals, Inc.)
- Subjects :
- Chemical Fractionation methods
Glucuronidase genetics
Hydrogen-Ion Concentration
Protein Engineering methods
Seeds enzymology
Seeds genetics
Glucuronidase biosynthesis
Glucuronidase isolation & purification
Pisum sativum enzymology
Pisum sativum genetics
Plants, Genetically Modified enzymology
Recombinant Proteins isolation & purification
Recombinant Proteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0006-3592
- Volume :
- 86
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Biotechnology and bioengineering
- Publication Type :
- Academic Journal
- Accession number :
- 15007847
- Full Text :
- https://doi.org/10.1002/bit.20039