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Raghava, S., Barua, B., Singh, P.K., Das, M., Madan, L., Bhattacharyya, S., Bajaj, K., Gopal, B., Varadarajan, R., Gupta, M.N. (2008). Refolding and simultaneous purification by three-phase partitioning of recombinant proteins from inclusion bodies.  Protein Sci. 17(11): 1987--1997.
FlyBase ID
FBrf0215772
Publication Type
Research paper
Abstract

Many recombinant eukaryotic proteins tend to form insoluble aggregates called inclusion bodies, especially when expressed in Escherichia coli. We report the first application of the technique of three-phase partitioning (TPP) to obtain correctly refolded active proteins from solubilized inclusion bodies. TPP was used for refolding 12 different proteins overexpressed in E. coli. In each case, the protein refolded by TPP gave either higher refolding yield than the earlier reported method or succeeded where earlier efforts have failed. TPP-refolded proteins were characterized and compared to conventionally purified proteins in terms of their spectral characteristics and/or biological activity. The methodology is scaleable and parallelizable and does not require subsequent concentration steps. This approach may serve as a useful complement to existing refolding strategies of diverse proteins from inclusion bodies.

PubMed ID
PubMed Central ID
PMC2578805 (PMC) (EuropePMC)
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Secondary IDs
    Language of Publication
    English
    Additional Languages of Abstract
    Parent Publication
    Publication Type
    Journal
    Abbreviation
    Protein Sci.
    Title
    Protein Science
    Publication Year
    1992-
    ISBN/ISSN
    0961-8368
    Data From Reference
    Genes (5)