Steric protection of a modified glass surface with adsorbed polyacrylamide: interactions with blood proteins.

Date publication

juin 1988

Journal

Journal of chromatography

Auteurs

Membres identifiés du Cancéropôle Est :
Dr VOEGEL Jean-Claude

Tous les auteurs :
Voegel JC, Pefferkorn E, Schmitt A

Lien Pubmed

https://www.ncbi.nlm.nih.gov/pubmed/3170671

Résumé

Glass beads chemically modified with aluminol (A1OH) groups were coated with a monolayer of high-molecular-mass polyacrylamide at different temperatures and exposed to 125I-labelled albumin and fibrinogen solutions for 1 h. No adsorption of albumin was observed, whereas fibrinogen adsorption increased as a function of temperature. These observations were interpreted in terms of the density and stability of the adsorbed polymer layer. At 25 degrees C, where fibrinogen adsorption was already important, it was shown, using 3H-labelled polyacrylamide, that fibrinogen partly displaced the polymer from its adsorption sites.

Mots clés

Acrylic Resins, Adsorption, Blood Proteins, analysis, Buffers, Chemical Phenomena, Chemistry, Fibrinogen, analysis, Glass, Humans, Surface Properties, Temperature

Référence

J. Chromatogr.. 1988 Jun;428(1):17-24