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Protein downstream processing: Design, Development And Application of High and Low-Resolution Methods (N. Labrou Ed.) 2nd edition

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    0540021 - ÚMG 2023 RIV US eng M - Monography Chapter
    Dráber, Pavel - Sulimenko, Tetyana - Sulimenko, Vadym - Dráberová, Eduarda
    Stabilization of proteins by freeze-drying in the presence of trehalose: a case study of tubulin.
    Protein downstream processing: Design, Development And Application of High and Low-Resolution Methods (N. Labrou Ed.) 2nd edition. New York: Humana Press, 2021, s. 417-435. ISBN 978-1-0716-0775-6
    R&D Projects: GA ČR(CZ) GA18-27197S; GA ČR(CZ) GA19-20716S; GA MŠMT(CZ) LTAUSA17052
    Institutional support: RVO:68378050
    Keywords : freeze-drying * trehalose * tubulin
    OECD category: Biochemistry and molecular biology
    https://link.springer.com/protocol/10.1007%2F978-1-0716-0775-6_27

    Microtubules, polymers of the heterodimeric protein αβ-tubulin, are indispensable for many cellular
    activities such as maintenance of cell shape, division, migration, and ordered vesicle transport. In vitro
    assays to study microtubule functions and their regulation by associated proteins require the availability of assembly-competent purified tubulin. However, tubulin is a thermolabile protein that rapidly converts into a nonpolymerizing state. For this reason, it is usually stored at -80 C or liquid nitrogen to preserve its conformation and polymerization properties. In this chapter, we describe a method for freeze-drying of assembly-competent tubulin in the presence of nonreducing sugar trehalose, and methods enabling the evaluation of tubulin functions in rehydrated samples.

    Permanent Link: http://hdl.handle.net/11104/0317697

     
     
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