Protein Refolding using Aqueous Two-Phase Systems

Author

Daniel Forciniti, Missouri University of Science and TechnologyFollow

Abstract

We present a novel refolding technique in which aqueous two-phase systems are used to both dissociate protein aggregates (inclusion bodies) and to refold the protein in only one operation. Three denaturant salts (sodium thiocyanate, calcium chloride, and lithium bromide) were used as phase-forming salts with poly(ethylene glycol) (PEG). We have tested the technique by dissolving carbonic anhydrase II aggregates and refolding the denatured protein in PEG-NaCI-NaSCN systems. © 1994.

Recommended Citation

D. Forciniti, "Protein Refolding using Aqueous Two-Phase Systems," Journal of Chromatography A, vol. 668, no. 1, pp. 95 - 100, Elsevier, May 1994.

The definitive version is available at https://doi.org/10.1016/0021-9673(94)80096-0

Department(s)

Chemical and Biochemical Engineering

International Standard Serial Number (ISSN)

0021-9673

Document Type

Article - Journal

Document Version

Citation

File Type

text

Language(s)

English

Rights

© 2024 Elsevier, All rights reserved.

Publication Date

06 May 1994