Improved Refolding of an Immobilized Fusion Protein

Author:

Stempfer Günter,Höll-Neugebauer Bärbel,Rudolph Rainer

Publisher

Springer Science and Business Media LLC

Subject

Biomedical Engineering,Molecular Medicine,Applied Microbiology and Biotechnology,Bioengineering,Biotechnology

Reference25 articles.

1. Marston, F.A.O. 1986. The purification of eukaryotic polypeptides synthesized in Escherichia coli. Biochemistry J. 240: 1–12

2. Rudolph, R. 1990 Renaturation of recombinant, disulfide-bonded proteins from “inclusion bodies,” p. 149–171 in Modern Methods in Protein and Nucleic Acid Research. H. Tschesche (ed), Walter de Gruyter, Berlin, New York.

3. Rudolph, R. 1996. Successful protein folding on an industrial scale, in Principles & Practice of Protein Engineering, J. L. Cleland & C. S. Craik (eds), J. Wiley & Sons, Inc., New York In press.

4. Kiefhaber, T., Rudolph, R., Kohler, H.-H. and Buchner, J. 1991. Protein aggregation in vitro and in vivo: A quantitative model of the kinetic competition between folding and aggregation. Bio/Technology 9: 825–829.

5. Höll-Neugebauer, B., Rudolph, R., Schmidt, M. and Buchner, J. 1991. Reconstitute of a heat shock effect in vitro Influence of GroE on the thermal aggregation of α-glucosidase from yeast. Biochemistry 30: 11609–11614.

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