Artículos de revistas
Effect of surface hydrophobicity distribution on retention of ribonucleases in hydrophobic interaction chromatography
Date
2004-07-16Registration in:
JOURNAL OF CHROMATOGRAPHY A 1043 (1): 47-55 JUL 16 2004
0021-9673
Author
Mahn Osses, Andrea
Lienqueo Contreras, María Elena
Asenjo de Leuze, Juan
Institutions
Abstract
The effect of surface hydrophobicity distribution of proteins on retention in hydrophobic interaction chromatography (HIC) was investigated. Average surface hydrophobicity as well as hydrophobic contact area between protein and matrix were estimated using a classical thermodynamic model. The applicability of the model to predict protein retention in HIC was investigated on ribonucleases with similar average surface hydrophobicity but different surface hydrophobicity distribution. It was shown experimentally that surface hydrophobicity distribution could have an important effect on protein retention in HIC. The parameter "hydrophobic contact area," which comes from the thermodynamic model, was able to represent well the protein retention in HIC with salt gradient elution. Location and size of the hydrophobic patches can therefore have an important effect on protein retention in HIC, and the hydrophobic contact area adequately describes this.