Purification of recombinant proteins by fusion with thermally-responsive polypeptides.
Publication
, Journal Article
Meyer, DE; Chilkoti, A
Published in: Nat Biotechnol
November 1999
Elastin-like polypeptides (ELPs) undergo a reversible, inverse phase transition. Below their transition temperature (Tt), ELPs are soluble in water, but when the temperature is raised above Tt, phase transition occurs, leading to aggregation of the polypeptide. We demonstrate a method for purification of soluble fusion proteins incorporating an ELP tag. Advantages of this method, termed "inverse transition cycling," include technical simplicity, low cost, ease of scale-up, and capacity for multiplexing. More broadly, the ability to environmentally modulate the physicochemical properties of recombinant proteins by fusion with ELPs will allow diverse applications in bioseparation, immunoassays, biocatalysis, and drug delivery.
Duke Scholars
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Published In
Nat Biotechnol
DOI
ISSN
1087-0156
Publication Date
November 1999
Volume
17
Issue
11
Start / End Page
1112 / 1115
Location
United States
Related Subject Headings
- Thioredoxins
- Recombinant Proteins
- Peptides
- Molecular Sequence Data
- Elastin
- Base Sequence
- Amino Acid Sequence
Citation
APA
Chicago
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MLA
NLM
Meyer, D. E., & Chilkoti, A. (1999). Purification of recombinant proteins by fusion with thermally-responsive polypeptides. Nat Biotechnol, 17(11), 1112–1115. https://doi.org/10.1038/15100
Meyer, D. E., and A. Chilkoti. “Purification of recombinant proteins by fusion with thermally-responsive polypeptides.” Nat Biotechnol 17, no. 11 (November 1999): 1112–15. https://doi.org/10.1038/15100.
Meyer DE, Chilkoti A. Purification of recombinant proteins by fusion with thermally-responsive polypeptides. Nat Biotechnol. 1999 Nov;17(11):1112–5.
Meyer, D. E., and A. Chilkoti. “Purification of recombinant proteins by fusion with thermally-responsive polypeptides.” Nat Biotechnol, vol. 17, no. 11, Nov. 1999, pp. 1112–15. Pubmed, doi:10.1038/15100.
Meyer DE, Chilkoti A. Purification of recombinant proteins by fusion with thermally-responsive polypeptides. Nat Biotechnol. 1999 Nov;17(11):1112–1115.
Published In
Nat Biotechnol
DOI
ISSN
1087-0156
Publication Date
November 1999
Volume
17
Issue
11
Start / End Page
1112 / 1115
Location
United States
Related Subject Headings
- Thioredoxins
- Recombinant Proteins
- Peptides
- Molecular Sequence Data
- Elastin
- Base Sequence
- Amino Acid Sequence