dc.creatorMahn Osses, Andrea
dc.creatorLienqueo Contreras, María Elena
dc.creatorAsenjo de Leuze, Juan
dc.date.accessioned2007-05-07T15:44:58Z
dc.date.accessioned2019-04-25T23:45:42Z
dc.date.available2007-05-07T15:44:58Z
dc.date.available2019-04-25T23:45:42Z
dc.date.created2007-05-07T15:44:58Z
dc.date.issued2004-07-16
dc.identifierJOURNAL OF CHROMATOGRAPHY A 1043 (1): 47-55 JUL 16 2004
dc.identifier0021-9673
dc.identifierhttp://repositorio.uchile.cl/handle/2250/124553
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/2428882
dc.description.abstractThe 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.
dc.languageen
dc.publisherELSEVIER
dc.subjectCRYSTAL-STRUCTURES
dc.titleEffect of surface hydrophobicity distribution on retention of ribonucleases in hydrophobic interaction chromatography
dc.typeArtículos de revistas


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