title: Adsorptive immobilization of erythrocyte membrane.
abstract: Immobilization of human erythrocyte membrane was carried out by adsorption on Fractosil, a porous form of silica. Acetylcholinesterase (AChE) was chosen as a representative membrane enzyme in this study. Dependency of adsorption on membrane concentration was determined. Positive cooperative interactions that occurred in the process of immobilization increased stability. Presence of hydrophobic ligands on derivatized Fractosil was found to enhance stability of immobilized preparations making them more effective for use in continuous catalytic transformations. It is suggested that adsorptive immobilization of membrane structures such as the human erythrocyte membrane fragments on Fractosil and other inexpensive supports may provide a convenient procedure for utilization of their catalytic potential. Such preparations may be used in diagnostic kits or for construction of biosensors.
authors.affiliation: Institute of Biochemistry and Biophysics, University of Tehran, PO Box 13145-1348, Tehran, Iran.
authors.forename: M
authors.initials: M
authors.lastname: Taghvaei
authors.forename: S
authors.initials: S
authors.lastname: Khezre-Barati
authors.forename: F
authors.initials: F
authors.lastname: Jalilvand
authors.forename: M
authors.initials: M
authors.lastname: Nemat-Gorgani
mesh_terms: D000110:Acetylcholinesterase / Q000378:metabolism*; D000327:Adsorption; D002384:Catalysis; D004800:Enzymes, Immobilized / Q000378:metabolism*; D004910:Erythrocyte Membrane / Q000201:enzymology*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D012822:Silicon Dioxide
chemical_list: D004800:Enzymes, Immobilized; D012822:Silicon Dioxide; D000110:Acetylcholinesterase