Sequential elution of proteins bound by hydrophobic interaction chromatography at subzero temperatures

Fractionation and recovery of whey proteins by hydrophobic interaction chromatography.

A method for the recovery and fractionation of whey proteins from a whey protein concentrate (80%, w/w) by hydrophobic interaction chromatography is proposed. Standard proteins and WPC 80 dissolved in phosphate buffer with ammonium sulfate 1 M were loaded in a HiPrep Octyl Sepharose FF column coupled to a fast protein liquid chromatography (FPLC) system and eluted by decreasing the ionic streng...

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...

Hydrophobic Affinity Chromatography of Proteins

1. Chromatographic studies have been made of the affinities of a number of purified proteins for agarose (Sepharose 4B) substituted with 4-phenylbutylamine (PBA) or with E-aminocaproyl-n-tryptophan methyl ester (ACTME) as compared to controls of untreated agarose and/or of cyanogen bromide treated agarose without addition of a substituting amine. 2. At pH 8, cu-chymotrypsin (3.4.4.5) and 7s y-g...