Polyethylene was examined as stationary phases for reversed-phase liquid chromatography of peptides. The selectivity for the separation of substance P and GnRH diastereoisomers on polyethylene stationary phases was compared with that for separation on alkyl-bonded silica and porous poly(styrene divinylbenzene). In contrast to alkyl-bonded silica polyethylene and polypropylene columns, having hydrophobic surfaces without polar groups, are stable over the wide pH range of 1#x2013;14, allowing the effective regeneration of the stationary phases, especially for peptides and proteins in preparative work. It is shown that GnRH, substance P, magainine-II-amide, fibrinogen peptides prepared by solid-phase method and semisynthetic insulins can be purified to a high degree, wich demonstrates the usefulness of polyethylene columns for the purification of peptides.
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