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  • Title: Study on orientation of immunoglobulin G on protein G layer.
    Author: Bae YM, Oh BK, Lee W, Lee WH, Choi JW.
    Journal: Biosens Bioelectron; 2005 Jul 15; 21(1):103-10. PubMed ID: 15967357.
    Abstract:
    A comparative study of immunoglobulin G (IgG) immobilization was performed, both on a thiolated protein G layer, where this immobilization was due to affinity binding with an Fc fragment of IgG, and on 11-mercaptoundecanoic acid (11-MUA), where the immobilization was due to chemical bonding. The change of IgG layer formation on the two base layers as a function of the IgG concentration was investigated by surface plasmon resonance (SPR), atomic force microscopy (AFM) in a non-contact mode, and spectroscopic ellipsometry (SE). It was observed that the IgG layer was immobilized more evenly on the thiolated protein G layer than on the 11-MUA layer, based on the SPR measurements. The surface topology analysis by AFM indicated that the IgG layer was immobilized on the protein G layer according to the envelope profile of the base layer. Based on the SE analysis, it was determined that the IgG layer thickness on the thiolated protein G layer increased with increasing IgG concentration. Based on the above analyses, the scheme for orientation of IgG immobilized on the thiolated protein G layer was proposed.
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