title: Cell surface interactions with metal chelates.
abstract: We have explored immobilized metal ion affinity adsorption as a means of discrimination between cells and to assess partially the types of interaction that might contribute to the adsorption of cells on the such adsorbents. Erythrocytes from different sources were adsorbed on immobilized iminodiacetic acid charged with Cu2+, Ni2+ or Zn2+. The affinity of the human erythrocytes for the immobilized metal ions follows the order Cu2+ greater than Ni2+ greater than Zn2+. The adsorption capacity of the rat erythrocytes decreased in the following order: Zn2+ greater than Ni2+ greater than Cu2+. Pre-saturation of the columns with imidazole lead to the recovery of over 90% of the cells applied on the columns. Enzymic removal of sialic acid residues from the surface of erythrocytes has no effect on the adsorption-elution profiles of these cells on affinity adsorbents. These findings suggest that histidine residues localized on the cell surface are involved in the cell binding to the adsorbent. This new separation principle could be expanded to other types of cell. It could be used as a diagnostic tool and for separation, as well as for probing cell surfaces.
authors.affiliation: Département de Génie Biologique, Université de Technologie de Compiègne, France.
authors.forename: H G
authors.initials: HG
authors.lastname: Botros
authors.forename: M
authors.initials: M
authors.lastname: Vijayalakshmi
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002614:Chelating Agents / Q000378:metabolism*; D002853:Chromatography, Liquid; D004910:Erythrocyte Membrane / Q000378:metabolism*; D006021:Glycophorins / Q000032:analysis; D006801:Humans; D008670:Metals / Q000378:metabolism*; D008969:Molecular Sequence Data; D051381:Rats
chemical_list: D002614:Chelating Agents; D006021:Glycophorins; D008670:Metals