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Reversible and irreversible denaturation of proteins in chromatographic systems
Author(s) -
Wetlaufer D.B.
Publication year - 1988
Publication title -
makromolekulare chemie. macromolecular symposia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.257
H-Index - 76
eISSN - 1521-3900
pISSN - 0258-0322
DOI - 10.1002/masy.19880170104
Subject(s) - chymotrypsinogen , chemistry , lysozyme , chromatography , denaturation (fissile materials) , rnase p , trypsin , ion chromatography , urea , bovine serum albumin , biochemistry , chymotrypsin , enzyme , rna , gene , nuclear chemistry
Protein denaturation in typical chromatographic mobile phases is examined from kinetic and equilibrium viewpoints, preliminary to consideration of the binding of proteins to stationary phases. Protein binding to a stationary phase may result in concomitant stabilization or destabilization. Experiments to clarify mechanisms and/or to lead to stabilization of proteins against denaturation are discussed. Among the work to be discussed are the ion exchange chromatography of α‐chymotrypsinogen and hen egg lysozyme with mobile phases containing urea; reverse phase HPLC of RNase A and serum albumin with conventional mobile phases; and hydrophobic interaction chromatography of enolase, carbonic anhydrase, lysozyme, RNase A, and bovine pancreatic trypsin inhibitor, mediated by the surfactant CHAPS.