A comprehensive study to protein retention in hydrophobic interaction chromatography

A comprehensive study to protein retention in hydrophobic interaction chromatography.

The effect of different kosmotropic/chaotropic salt systems on retention characteristics of intact proteins has been examined in hydrophobic interaction chromatography (HIC). The performance was assessed using different column chemistries, i.e., polyalkylamide, alkylamine incorporating hydrophobic moieties, and a butyl chemistry. Selectivity in HIC is mainly governed by the salt concentration a...

Prediction of Retention time of hydrophobic peptide tagged cutinases in Hydrophobic Interaction Chromatography

Hydrophobic interaction chromatography (HIC) is an important technique for protein purification, which exploits the separation of proteins based on hydrophobic interactions between the stationary phase ligands and hydrophobic regions on the protein surface. One way of enhancing the purification efficiency by HIC is the addition of short sequences of peptide tags to the target protein by genetic...

Hydrophobic Interaction Chromatography

Hydrophobic Interaction Chromatography

modeling for the design of a Biomimetic chimeric ligand. Application to the puriRcation of bovine heart L-lactate dehydrogenase. Biotechnology and Bioengineering 63: 321}331. Lowe CR (1984) Applications of reactive dyes in biotechnology. In: Wiseman A (ed.) Topics in Enzyme and Fermentation Biotechnology, vol. 9. Chichester: Ellis Horwood. Lowe CR, Burton S, Pearson J, Clonis YD and Stead CV (1...

Hydrophobic Interaction Chromatography.

Most proteins and large polypeptides have hydrophobic regions at their surface. These hydrophobic "patches" are due to the presence of the side chains of hydrophobic or nonpolar amino acids such as phenylalanine, tryptophan, alanine, and methionine. These surface hydrophobic regions are interspersed between more hydrophilic or polar regions and the number, size, and distribution of them is a sp...