Affinity surfactants as reversibly bound ligands for high-performance affinity chromatography

J. L. Torres, R. Guzman, R. G. Carbonell, P. K. Kilpatrick

Research output: Contribution to journalArticlepeer-review

15 Scopus citations


Pyridine was coupled covalently to a nonionic ethoxylated alcohol: octaethylene glycol n-hexadecyl ether. This modified surfactant was found to be a reversible, competitive inhibitor of horse serum cholinesterase. The surfactant bound irreversibly, in aqueous media, to octadecylbonded reverse phase silica particles commonly used for high-performance liquid chromatography. The amount of ligand bound was found to be 550 μmol/ml of packing, a concentration that is over 100 times higher than what can be normally bound to agarose affinity chromatography supports. With this packing, a 280-fold purification of cholinesterase from horse serum and a 79-fold purification of human serum cholinesterase were accomplished, with yields greater than 80%, using a 2-cm-long column and a 7-min elution time. The affinity surfactant could be eluted from the column using a 6:4 (v/v) mixture of methanol and isopropanol. This technique should be generally applicable in the development of biospecific supports for high-performance affinity chromatography.

Original languageEnglish (US)
Pages (from-to)411-418
Number of pages8
JournalAnalytical Biochemistry
Issue number2
StatePublished - Jun 1988
Externally publishedYes


  • affinity-labeled surfactants
  • high-performance affinity chromatography
  • ligand immobilization
  • Nonionic surfactants
  • octadecyl-bonded silica
  • serum cholinesterase

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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