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    Reversible detection of proteases and their inhibitors by a pulsed chronopotentiometric polyion-sensitive electrode

    20847_downloaded_stream_303.pdf (70.52Kb)
    Access Status
    Open access
    Authors
    Xu, Y.
    Shvarev, A.
    Makarychev-Mikhailov, S.
    Bakker, Eric
    Date
    2008
    Type
    Journal Article
    
    Metadata
    Show full item record
    Citation
    Xu, Yida and Shvarev, Alexey and Makarychev-Mikhailov, Sergey and Bakker, Eric. 2008. Reversible detection of proteases and their inhibitors by a pulsed chronopotentiometric polyion-sensitive electrode. Analytical Biochemistry 374 (2): 366-370.
    Source Title
    Analytical Biochemistry
    DOI
    10.1016/j.ab.2007.10.043
    Faculty
    Nanochemistry Research Centre
    School
    Nanochemistry Research Institute (Research Institute)
    Remarks

    Xu, Yida and Shvarev, Alexey and Makarychev-Mikhailov, Sergey and Bakker, Eric (2008) Reversible detection of proteases and their inhibitors by a pulsed chronopotentiometric polyion-sensitive electrode, Analytical Biochemistry 374(2):366-370.

    The link to this article is:

    http://dx.doi.org/10.1016/j.ab.2007.10.043

    Copyright 2008 Elsevier B.V. All rights reserved

    URI
    http://hdl.handle.net/20.500.11937/46682
    Collection
    • Curtin Research Publications
    Abstract

    Polymer membrane electrodes operated by pulsed chronopotentiometry have recently been introduced to replace traditional ion-selective electrodes for a number of applications. While ion-selective electrodes for the polycation protamine have been reported, for instance, a pulsed chronopotentiometric readout mode (called here pulstrode) provides improved stability and reproducibility while exhibiting sufficient selectivity for the direct detection of protamine in undiluted whole blood samples. Here, such protamine-sensitive pulstrodes are applied for the real-time detection of the activity of the protease trypsin and its soybean inhibitor. This is possible because small fragments produced by the trypsin digestion are not detectable by the protamine-sensing membrane. The real-time response to the proteolytic reaction is shown to exhibit good reproducibility and reversibility, and the initial reaction rate is dependent on the concentration of the protease and its inhibitor.

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