PMID: 1254Nov 15, 1975

The renaturation of reduced polyalanyl-chymotrypsinogen and chymotrypsinogen

European Journal of Biochemistry
G OrsiniM E Goldberg

Abstract

Chymotrypsinogen has been successfully renatured in solution, after reduction of its 5 disulfide bonds in 6 M guanidine-HCl. This has been made possible by the study of the renaturation of a model derivative, polyalanyl-chymotrypsinogen. The reduced derivative is shown to refold and reoxodize spontaneously, with a 30-40% yield, into molecules which are monomeric and fully susceptible to activation by trypsin. Chymotrypsinogen can also be renatured but only in the presence of reagents allowing disulfide interchange and of moderate concentrations of guanidine-HCl or urea. These results illustrate how the kinetic trapping of incorrectly folded molecules by wrong S-S bonds and aggregation can be overcome, thus allowing the correct refolding of the protein.

References

Mar 27, 1975·Nature·C Chothia
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Citations

Jan 1, 1978·Progress in Biophysics and Molecular Biology·T E Creighton
Jan 1, 1994·Biotechnology Advances·B E Fischer
Mar 15, 2000·Protein Science : a Publication of the Protein Society·D SamuelC Yu
Jun 30, 2005·Médecine sciences : M/S·M E Goldberg
Sep 8, 1987·Biochemistry·J K SwadeshH A Scheraga
Jul 19, 1996·The Journal of Biological Chemistry·B RamanC M Rao

Related Concepts

Abufne
Chymotrypsinogen beta
Reduced Glutathione
Guanidines
Hydrogen-Ion Concentration
Oxidation-Reduction
Polynucleotides
Plasma Protein Binding Capacity
Protein Conformation
Protein Denaturation

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