Ionic binding of human serum albumin - Dependence on pH and ionic strength: A chromatographic approach

Citation
Yc. Guillaume et al., Ionic binding of human serum albumin - Dependence on pH and ionic strength: A chromatographic approach, CHROMATOGR, 52(9-10), 2000, pp. 575-578
Citations number
40
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Chemistry & Analysis","Spectroscopy /Instrumentation/Analytical Sciences
Journal title
CHROMATOGRAPHIA
ISSN journal
0009-5893 → ACNP
Volume
52
Issue
9-10
Year of publication
2000
Pages
575 - 578
Database
ISI
SICI code
0009-5893(200011)52:9-10<575:IBOHSA>2.0.ZU;2-3
Abstract
A chemometric method was applied to investigate the binding mechanism of Ca 2+ and Mg2+ to human serum albumin (HSA) using a bio-chromatographic approa ch. The effects of the bulk solvent pH, its ionic strength and column tempe rature on the transfer of Ca2+ and Mg2+ from the bulk solvent to immobilize d human serum albumin as a stationary phase were studied, Thermodynamic par ameters corresponding to this transfer were determined from linear van't Ho ff plots. Enthalpy-entropy compensation revealed that the ion binding mecha nism to HSA was independent of ionic strength and pH, and the same for the two cations. The results corroborated the fact that HSA can be assimilated by a weak cation-exchanger and the Ca-HSA (or Mg-HSA) binding is controlled by electrostatic attraction for different "non specific" areas of serum al bumin.