• Something wrong with this record ?

Stabilization of Proteins by Freeze-Drying in the Presence of Trehalose: A Case Study of Tubulin

P. Dráber, V. Sulimenko, T. Sulimenko, E. Dráberová

. 2021 ; 2178 (-) : 417-435. [pub] -

Language English Country United States

Document type Journal Article, Research Support, Non-U.S. Gov't

Persistent link   https://www.medvik.cz/link/bmc21011678

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.

References provided by Crossref.org

000      
00000naa a2200000 a 4500
001      
bmc21011678
003      
CZ-PrNML
005      
20210507103558.0
007      
ta
008      
210420s2021 xxu f 000 0|eng||
009      
AR
024    7_
$a 10.1007/978-1-0716-0775-6_27 $2 doi
035    __
$a (PubMed)33128764
040    __
$a ABA008 $b cze $d ABA008 $e AACR2
041    0_
$a eng
044    __
$a xxu
100    1_
$a Dráber, Pavel $u Laboratory of Biology of Cytoskeleton, Institute of Molecular Genetics of the Czech Academy of Sciences, Prague, Czech Republic. paveldra@img.cas.cz
245    10
$a Stabilization of Proteins by Freeze-Drying in the Presence of Trehalose: A Case Study of Tubulin / $c P. Dráber, V. Sulimenko, T. Sulimenko, E. Dráberová
520    9_
$a 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.
650    _2
$a lyofilizace $7 D005612
650    _2
$a lidé $7 D006801
650    _2
$a stabilita proteinů $7 D055550
650    _2
$a trehalosa $x chemie $7 D014199
650    _2
$a tubulin $x chemie $7 D014404
655    _2
$a časopisecké články $7 D016428
655    _2
$a práce podpořená grantem $7 D013485
700    1_
$a Sulimenko, Vadym $u Laboratory of Biology of Cytoskeleton, Institute of Molecular Genetics of the Czech Academy of Sciences, Prague, Czech Republic
700    1_
$a Sulimenko, Tetyana $u Laboratory of Biology of Cytoskeleton, Institute of Molecular Genetics of the Czech Academy of Sciences, Prague, Czech Republic
700    1_
$a Dráberová, Eduarda $u Laboratory of Biology of Cytoskeleton, Institute of Molecular Genetics of the Czech Academy of Sciences, Prague, Czech Republic
773    0_
$w MED00180389 $t Methods in molecular biology (Clifton, N.J.) $x 1940-6029 $g Roč. 2178, č. - (2021), s. 417-435
856    41
$u https://pubmed.ncbi.nlm.nih.gov/33128764 $y Pubmed
910    __
$a ABA008 $b sig $c sign $y p $z 0
990    __
$a 20210420 $b ABA008
991    __
$a 20210507103557 $b ABA008
999    __
$a ok $b bmc $g 1650142 $s 1132057
BAS    __
$a 3
BAS    __
$a PreBMC
BMC    __
$a 2021 $b 2178 $c - $d 417-435 $e - $i 1940-6029 $m Methods in molecular biology $n Methods Mol Biol $x MED00180389
LZP    __
$a Pubmed-20210420

Find record

Citation metrics

Archiving options