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Protein chromatography in neat organic solvents
Author(s) -
Chang Nancy,
Klibanov Alexander M.
Publication year - 1992
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260390513
Subject(s) - formamide , ethylene glycol , chemistry , adsorption , chromatography , ion chromatography , ion exchange , ribonuclease , ethylene , thermoresponsive polymers in chromatography , hydrophilic interaction chromatography , organic chemistry , ion , high performance liquid chromatography , catalysis , biochemistry , rna , gene
Pure formamide and ethylene glycol are used instead of water as processing media for protein chromatography. A number of common proteins are freely soluble in these solvents and most do not undergo irrersible inactivation in them. Batch adsorption studies reveal that proteins readily adsorbed to various ion‐exchangers in formamide and ethyline glycol and subsequently can be completely desorbed by adding inorganic salts (LiCl and NH 4 NO 3 ) to the solvents. The idea of protein separations in formamide and ethylene glycol is illustrated by column chromatography and preparative separation of mixtures of (i) oxidized A and B chains of insulin and (ii) lysozyme and ribonuclease on the anion‐exchanger triethylaminoethycellulose and the cation‐exchanger phosphocellulose, respectively.