Abstract
Abstract 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 1–14, 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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