Improved non-chromatographic purification of a recombinant protein by cationic elastin-like polypeptides
- Authors
- Lim, Dong Woo; Trabbic-Carlson, Kimberly; MacKay, J. Andrew; Chilkoti, Ashutosh
- Issue Date
- May-2007
- Publisher
- AMER CHEMICAL SOC
- Citation
- BIOMACROMOLECULES, v.8, no.5, pp.1417 - 1424
- Indexed
- SCIE
SCOPUS
- Journal Title
- BIOMACROMOLECULES
- Volume
- 8
- Number
- 5
- Start Page
- 1417
- End Page
- 1424
- URI
- https://scholarworks.bwise.kr/erica/handle/2021.sw.erica/43762
- DOI
- 10.1021/bm060849t
- ISSN
- 1525-7797
- Abstract
- This paper reports an improvement in the purification of thioredoxin (Trx) expressed from E. coli by inverse transition cycling (ITC) using cationic elastin-like polypeptides (ELPs). Two ELP libraries having 2% and 5% lysine residues and molecular weights ranging from 4 to 61.1 kDa showed greater salt sensitivity in their inverse transition behavior than purely aliphatic ELPs. Expression yield of Trx-ELP fusions was an unpredictable function of guest residue composition, but reducing the molecular weight of the ELP tag generally increased Trx yield. A cationic 4.3 kDa ELP is the shortest ELP used to purify any protein by ITC to date. A 15.9 kDa ELP with a guest residue composition of K:V:F of 1:7:1 was found to be the optimal cationic tag to purify Trx, as it provided 50% greater Trx yield and only required one-fifth the added NaCl for purification of Trx as compared to previously used aliphatic ELP tags.
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