Differences in retention behavior between small and large molecules in ion-exchange chromatography and reversed-phase chromatography

Ekström, Björn; Jacobson, Gunilla

doi:10.1016/0003-2697(84)90527-x

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1986

2010

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Cited by 9 publications

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“…IV-acetyl-Dglucosamine, ethyl caproate, diglycolic acid, succinic anhydride (SA), and diglycolic anhydride (DGA) were from Aldrich (Milwaukee, WI). Hypersil 100 and 300, 5-µ particle diameter, Nucleosil 300, 5 Mm, and LiChrospher SI300 and SI4000, 10 Mm, were from Alltech (Deerfield, IL). Dimethyl diglycolate was prepared from diglycolic acid and diazomethane using a Diazald kit (Aldrich).…”

Section: Methodsmentioning

confidence: 99%

Preparation of chromatographic supports of variable ligand density

Landgrebe¹,

Wu²,

Walters³

1986

Anal. Chem.

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Section: Methodsmentioning

confidence: 99%

Preparation of chromatographic supports of variable ligand density

Landgrebe¹,

Wu²,

Walters³

1986

Anal. Chem.

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Chromatography, Hydrophobic Interaction

Kårsnäs¹

1999

Encyclopedia of Bioprocess Technology

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Chromatography, Hydrophobic Interaction

Kårsnäs

2010

Encyclopedia of Industrial Biotechnology

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Hydrophobic interaction chromatography (HIC) is based on complex interactions between the separation media and biomolecules. This compexity is due to that the salt‐mediated mechanism for attraction in unusually dependent also on the individual sterical structures of the counterparts. A hydrophobic ligand thus may express different separation selectivitiy patterns when coupled to different media with different tecniques. Prediction of results therefore cannot be made based on experiments performed on another separation medium with the same ligand. HIC uses moderately hydrophobic ligands where the molecules to be separated are forced to attach to the columns by increasing the ionic strength of the eluent. It is mainly used for large biomolecules forming multipoint attraction with the medium. Elution is performed with gradients of decreasing ionic strength and short and wide columns are used to optimize the separation. Tertiary structures tend to be preserved but attached molecules should be eluted as soon as possible due to the risc of confomational changes and enhanced binding making elution difficult. An HIC medium may be characterized by the profile of elution data of a set of marker proteins using PCA making possible the comparision and classification of media and prediction of results. Optimization is facilitated by running the sample through columns eqilibrated with stepwise higher ionic strength.

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Differences in retention behavior between small and large molecules in ion-exchange chromatography and reversed-phase chromatography

Cited by 9 publications

References 4 publications

Preparation of chromatographic supports of variable ligand density

Preparation of chromatographic supports of variable ligand density

Chromatography, Hydrophobic Interaction

Chromatography, Hydrophobic Interaction

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