Purification of recombinant proteins by fusion with thermally-responsive polypeptides View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1999-11

AUTHORS

D E Meyer, A Chilkoti

ABSTRACT

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. More... »

PAGES

1112-1115

Journal

TITLE

Nature Biotechnology

ISSUE

11

VOLUME

17

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/15100

DOI

http://dx.doi.org/10.1038/15100

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1042379113

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/10545920


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