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EN
ČeštinaEnglish

Isolation of chimaeric forms of elongation factor EF-Tu by affinity chromatography.

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378050%3A_____%2F02%3A23033141" target="_blank" >RIV/68378050:_____/02:23033141 - isvavai.cz</a>

  • Result on the web

    —

  • DOI - Digital Object Identifier

    —

Alternative languages

  • Result language

    angličtina

  • Original language name

    Isolation of chimaeric forms of elongation factor EF-Tu by affinity chromatography.

  • Original language description

    Six different recombinant chimaeric forms of a three-domain protein, proteosynthetic elongation factor Tu (EF-Tu), composed of domains of EF-Tu of mesophilic (Escherichia coli) and thermophilic (Bacillus stearothermophilus) origin as well as free N-terminal domains of EF-Tu, and the whole recombinant EF-Tus of both organisms were prepared and isolated by the GST (glutathione S-transferase) fusion technology. Several modifications in the standard isolation and purification procedures are described that proved necessary to obtain the proteins in a purified and undegraded form.

  • Czech name

    —

  • Czech description

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Classification

  • Type

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

  • CEP classification

    EB - Genetics and molecular biology

  • OECD FORD branch

    —

Result continuities

  • Project

    <a href="/en/project/GA204%2F98%2F0863" target="_blank" >GA204/98/0863: Thermostability of proteins - mutagenesis of elongation factor Tu from Bacillus stearothermophilus</a><br>

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Others

  • Publication year

    2002

  • 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 Chromatography B

  • ISSN

    1570-0232

  • e-ISSN

    —

  • Volume of the periodical

    770

  • Issue of the periodical within the volume

    1-2

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    7

  • Pages from-to

    129-135

  • UT code for WoS article

    —

  • EID of the result in the Scopus database

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Similar results(10)

Thermostability of Multidomain Proteins: Properties of Chimaeric Elongation Factors EF-Tu Composed of Domains of Mesophilic-Escherichia coli EF-Tu and Thermophilic-Bacillus stearothermophilus EF-Tu.Thermostability of Multidomain Proteins Studied by Domain Swapping between Mesophilic-Escherichia coli and Thermophilic-Bacillus stearothermophilus Elongation Factors EF-Tu.Thermostability of Multidomain Proteins: Elongation Factors EF-Tu from Escherichia coli and Bacillus stearothermophilus and Their Chimeric Forms.