Format

Send to

Choose Destination
See comment in PubMed Commons below
J Chromatogr B Biomed Sci Appl. 1999 May 28;728(2):167-74.

Chromatographic study of magnesium and calcium binding to immobilized human serum albumin.

Author information

1
Laboratoire de Chimie Analytique, Faculté de Médecine et Pharmacie, Besançon, France.

Abstract

The use of immobilized human serum albumin (HSA) as a stationary phase in affinity chromatography has been shown to be useful in resolving optical antipodes or to investigate interactions between drugs and protein. However, to our knowledge, no inorganic ion binding has been studied on this immobilized protein type. To do this, the human serum albumin stationary phase was assimilated to a weak cation-exchanger by working with a mobile phase pH equal to 6.5. A study of the eluent ionic strength effect on ion retention was carried out by varying the buffer concentrations and the column temperatures. The thermodynamic parameters for magnesium and calcium transfer from the mobile to the stationary phase were determined from linear van't Hoff plots. An enthalpy-entropy compensation study revealed that the type of interaction was independent of the mobile phase composition. A simple model based on the Gouy-Chapman theory was considered in order to describe the retention behavior of the test cations with the mobile phase ionic strength. From this theoretical approach, the relative charge densities of the human serum albumin surface implied in the binding process were estimated at different column temperatures.

PMID:
10406202
[Indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Loading ...
    Support Center