Abstract
A series of packings that had alkyl and aryl groups incorporated into a hydrophilic polymeric matrix were developed for hydrophobic interaction chromatography. Using an inverse salt gradient of ammonium sulfate or sodium chloride, a series of proteins were purified and the activity of trypsin was monitored using post-column detection. Retention times of proteins generally increased in the following order of ligands: hydroxypropyl, propyl, benzyl, isopropyl, phenyl and pentyl.
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