1988/04/01 by D.B. Wetlaufer · 1 citation
Biochemistry, Genetics and Molecular Biology · Materials Science · #Protein purification and stability #Enzyme Structure and Function #Protein Structure and Dynamics
paper · doi:10.1002/masy.19880170104
openalex publication_date 1988/04/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/05/21
Abstract 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.