Specific salt effects in hydrophobic interaction chromatography of proteins

L. Szepesy, Cs Horváth

Research output: Article

25 Citations (Scopus)


It has been noted in the literature that certain salts enter into specific interaction with proteins. As a result of this, they may act as salting-in agents. We have investigated the effect of magnesium chloride which is known to possess such unusual properties on the retention of proteins in hydrophobic-interaction chromatography. First the retention behaviour of amino acids and small peptides having a wide polarity range was studied on reversed-phase columns using eluents containing (NH4)2SO4, MgSO4 or MgCl2, in wide the concentration ranges. For less polar eluites plots of the logarithmic retention factors against the salt concentration were found to be linear, whereas the more polar species showed irregular behavior. The retention of a wide range of proteins was measured on a TSK Phenyl-5-PW column using eluents containing (NH4)2SO4, MgSO4 or MgCl2 at different concentrations. The salt-mediated retention was regular with (NH4)2 SO4 and MgSO4 although MgSO4 showed a lesser effect than that predicted by the surface-tension increment. The effect of MgCl2 was quite irregular: the retention factors either increased or decreased or remained unchanged depending on the protein. These results corroborate earlier observations regarding the particular effect of MgCl2 and suggest the modulation of selectivity in hyrophobic-interaction chromatography by the addition of MgCl2 to the eluent.

Original languageEnglish
Pages (from-to)13-18
Number of pages6
Issue number1
Publication statusPublished - dec. 1 1988

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry
  • Clinical Biochemistry
  • Organic Chemistry

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