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Selective isolation of hydrophobin SC3 by solid-phase extraction with polytetrafluoroethylene microparticles and subsequent mass spectrometric analysis

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60162694%3AG44__%2F16%3A43875564" target="_blank" >RIV/60162694:G44__/16:43875564 - isvavai.cz</a>

  • Alternative codes found

    RIV/00216275:25310/16:39901585

  • Result on the web

    <a href="http://onlinelibrary.wiley.com/wol1/doi/10.1002/jssc.201500912/full" target="_blank" >http://onlinelibrary.wiley.com/wol1/doi/10.1002/jssc.201500912/full</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1002/jssc.201500912" target="_blank" >10.1002/jssc.201500912</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Selective isolation of hydrophobin SC3 by solid-phase extraction with polytetrafluoroethylene microparticles and subsequent mass spectrometric analysis

  • Original language description

    Hydrophobins are small proteins that play a role in a number of processes during the filamentous fungi growth and development. These proteins are characterized by the self-assembly of their molecules into an amphipathic membrane at hydrophilic-hydrophobic interfaces. Isolation and purification of hydrophobins generally present a challenge in their analysis. Hydrophobin SC3 from Schizophyllum commune was selected as a representative of class I hydrophobins in this work. A novel procedure for selective and effective isolation of hydrophobin SC3 based on solid-phase extraction with polytetrafluoroethylene microparticles loaded in a small self-made microcolumn is reported. The tailored binding of hydrophobins to polytetrafluoroethylene followed by harsh elution conditions resulted in a highly specific isolation of hydrophobin SC3 from the model mixture of ten proteins. The presented isolation protocol can have a positive impact on the analysis and utilization of these proteins including all class I hydrophobins. Hydrophobin SC3 was further subjected to reduction of its highly stable disulfide bonds and to chymotryptic digestion followed by mass spectrometric analysis. The isolation and digestion protocols presented in this work make the analysis of these highly hydrophobic and compact proteins possible.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CB - Analytical chemistry, separation

  • OECD FORD branch

Result continuities

  • Project

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2016

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Journal of Separation Science

  • ISSN

    1615-9306

  • e-ISSN

  • Volume of the periodical

    39

  • Issue of the periodical within the volume

    4

  • Country of publishing house

    DE - GERMANY

  • Number of pages

    8

  • Pages from-to

    717-724

  • UT code for WoS article

    000371163300012

  • EID of the result in the Scopus database