Hydrophobic interaction fast protein liquid chromatography of milk proteins

Abstract Bovine whey proteins and caseins were separated by hydrophobic interaction chromatography with the new Pharmacia fast protein liquid chromatography column, phenyl-Superose. Total casein was separated using a decreasing gradient of 0.8 to 0.05 M sodium phosphate and a constant 3.75 M urea concentration at pH 6.0. The order of elution of caseins was β s2 s1 , and β-casein was always eluted first. Whey proteins were separated with a decreasing salt gradient of 1.5 to 0 M ammonium sulphate in 0.05 M sodium phosphate at ph 7.0. The order of elution was β-lactoglobulin