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  • 1
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Advanced Materials for Optics and Electronics 8 (1998), S. 101-105 
    ISSN: 1057-9257
    Keywords: biosensor ; protein immobilisation ; protein modification ; electrochemistry ; nitrotyrosine ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Electrical Engineering, Measurement and Control Technology , Physics
    Notes: Use of electrosynthetic methodology allows the production of hen egg-white lysozyme (HEWL) either mononitrated at tyrosine 23 or bisnitrated at tyrosines 20 and 23, but never nitrated at tyrosine 53. This is a different sequence from that obtained by the chemical nitrating agent tetranitromethane, and when reduced by dithionite, the selectively modified enzyme can be anchored at pH 5 via the unique aromatic amino group to magnetic beads or other suitable matrices. HEWL so immobilised loses less than 10% of cell-wall lytic activity compared with the approximately 50% loss of activity when immobilised by conventional methodology at pH 9 via essentially random reaction at lysine residues and other functionalities which are nucleophilic at this pH. This result offers promise as a general method for selective protein immobilisation in biosensors and similar applications. © 1998 John Wiley & Sons, Ltd.
    Additional Material: 1 Tab.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Advanced Materials for Optics and Electronics 8 (1998), S. 47-52 
    ISSN: 1057-9257
    Keywords: ligand gated ; channel protein ; biomembrane ; biosensor ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Electrical Engineering, Measurement and Control Technology , Physics
    Notes: We demonstrate a novel protective configuration for a gated channel biosensor. The bilayer membrane containing the channel proteins is formed by a simple self-assembly technique ensuring continuous coverage of the interface between two slabs of agarose gel by a biomimetic lamella in a fluid state. The gel protects both membrane surfaces from mechanical shock and contact with low-energy media while allowing diffusion of biomolecules up to 10 MDa in weight. The technique has been demonstrated using both dioleoyl-phosphatidylcholine (DOPC) and a phosphatidylcholine lipid cross-linked with a short polysiloxane chain (PSPC). The conductance per unit area of the channel-free membrane produced by this method was less than 25 S m-2 for DOPC and 2 S m-2 for PSPC, and the bilayer nature of the barrier in both cases has been demonstrated by measurement of the capacitance. The applicability to sensors has been confirmed using gramicidin-D, a 1·1 kDa unilamellar lipid bilayer pore former, and partially confirmed using valinomycin, a selective ion transporter. On incorporation of gramicidin the membrane conductance increased by over an order of magnitude. © 1998 John Wiley & Sons, Ltd.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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