High-performance liquid chromatography of amino acids, peptides and proteins. LXXXVIII. Calculation of the average distance between protein solutes and the stationary phase during isocratic anion-exchange chromatography

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This investigation deals with protein retention behaviour in high-performance anion-exchange chromatography in terms of the average distance of approach between the protein solute and the positively charged anion-exchange stationary-phase surface. The theoretical treatment is based on a modified Debye-Hückel theory for spherical impenetrable ions, where the electrostatic potential energy has been related to the chromatographic capacity factor, k′. Results are presented for three globular proteins, eluted isocratically from a Mono-Q strong anion-exchange resin with sodium choride as the displacer salt by a mobile phase with pH in the range 5.50-9.60. Analysis of experimental retention data indicates that topographically predefined, charged regions on the protein surface, called ionotopes, control the orientation and approach distance of the protein solute.

Original languageEnglish
Pages (from-to)45-56
Number of pages12
JournalJournal of Chromatography A
Issue numberC
Publication statusPublished - 23 Dec 1988

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