AN ADAPTATION OF HYDROPHOBIC INTERACTION CHROMATOGRAPHY FOR ESTIMATION OF PROTEIN SOLUBILITY OPTIMA

Citation
P. Gagnon et al., AN ADAPTATION OF HYDROPHOBIC INTERACTION CHROMATOGRAPHY FOR ESTIMATION OF PROTEIN SOLUBILITY OPTIMA, Journal of pharmaceutical and biomedical analysis, 16(4), 1997, pp. 587-592
Citations number
19
Language
INGLESE
art.tipo
Article
ISSN journal
0731-7085
Volume
16
Issue
4
Year of publication
1997
Pages
587 - 592
Database
ISI
SICI code
0731-7085(1997)16:4<587:AAOHIC>2.0.ZU;2-8
Abstract
This study describes and adaptation of hydrophobic interaction chromat ography (HIC) that can be used to estimate protein solubility optima. The method does not support determination of absolute, e.g. quantitati ve solubility, however it does provide a basis for identifying the sal t concentration, pH, or additive concentrations that support the highe st relative solubility. The magnitude of a given salt's effects are co nsistent with its ranking in the Hofmeister series. IgG in solutions o f strong 'precipitating' salts exhibits a classical salting-in/salting -out curve, described by a solubility minimum at low ionic strength, i ncreasing to a well-defined maximum, and then losing solubility with f urther elevation of salt concentration. The direct effect of pH on pro tein solubility, as well as its indirect effect via modification of th e ionic equilibria of dissolved salts, can also be tracked. Cooperativ e effects of solubility modifiers such as amino acids can likewise be assessed. The technique can be a useful tool in the development of liq uid formulations for protein pharmaceuticals. (C) 1997 Elsevier Scienc e B.V.