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    Wyświetlanie 1-4 z 4
    Tytuł:
    A freeze-thaw method for disintegration of Escherichia coli cells producing T7 lysozyme used in pBAD expression systems
    Autorzy:
    Wanarska, Marta
    Hildebrandt, Piotr
    Kur, Józef
    Powiązania:
    https://bibliotekanauki.pl/articles/1041062.pdf
    Data publikacji:
    2007
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    pBAD expression systems
    disintegration
    T7 lysozyme
    Opis:
    The pLysN plasmid containing the T7 lysozyme gene under control of the lac promoter was constructed to facilitate cell disintegration after expression of recombinant proteins in arabinose-induced expression systems. The usefulness of this plasmid was tested in Escherichia coli TOP10 and E. coli LMG194 cells carrying pBADMHADgeSSB plasmid containing Deinococcus geothermalis SSB protein gene under control of the araBAD promoter. The results showed that low-level expression of T7 lysozyme did not interfere with the target SSB protein production, and that the freezing-thawing treatment was sufficient for disruption of the E. coli cells producing low amounts of T7 lysozyme.
    Źródło:
    Acta Biochimica Polonica; 2007, 54, 3; 671-672
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Thermostable Pyrococcus woesei β-D-galactosidase - high level expression, purification and biochemical properties
    Autorzy:
    Wanarska, Marta
    Kur, Józef
    Pladzyk, Radosław
    Turkiewicz, Marianna
    Powiązania:
    https://bibliotekanauki.pl/articles/1041317.pdf
    Data publikacji:
    2005
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    Pyrococcus woesei
    β-d-galactosidase
    Escherichia coli
    purification
    expression system
    Opis:
    The gene encoding β-D-galactosidase from Pyrococcus woesei was PCR amplified, cloned, expressed in Escherichia coli under the control of an inducible T7 promoter, purified and characterized. The expression system was developed by the construction of recombinant plasmid, based on the high copy number pUET1 vector, giving four times more efficient expression of P. woesei β-D-galactosidase (20 mg of enzyme from 1 liter of culture) than that obtained from a previously constructed one. The recombinant enzymes were purified in a two-step procedure: double heat-denaturation of E. coli cell proteins and affinity chromatography on p-aminobenzyl 1-thio-β-D-galactopyranoside-agarose. To achieve efficient purification of P. woesei β-D-galactosidase by immobilized metal-ion affinity chromatography (IMAC), a His-tag was placed either at the N- or the C-terminal of the coding sequence. The obtained fusion proteins revealed the same specific activity of approximately 5400 U/mg, which was 10 times lower than the wild-type β-D-galactosidase (51100 U/mg). The activity of P. woesei β-D-galactosidase was enhanced by thiol compounds, Mg2+ ions and D-galactose, and was inhibited by heavy metal ions and D-glucose, while Ca2+ ions had no effect.
    Źródło:
    Acta Biochimica Polonica; 2005, 52, 4; 781-787
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Single-stranded DNA-binding proteins (SSBs) - sources and applications in molecular biology.
    Autorzy:
    Kur, Józef
    Olszewski, Marcin
    Filipkowski, Paweł
    Powiązania:
    https://bibliotekanauki.pl/articles/1041357.pdf
    Data publikacji:
    2005
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    Thermus aquaticus
    Thermus thermophilus
    Escherichia coli
    PCR
    recombination
    DNA replication
    SSB
    Opis:
    Single-stranded DNA-binding proteins (SSBs) play essential roles in DNA replication, recombination, and repair in bacteria, archaea and eukarya. The SSBs share a common core ssDNA-binding domain with a conserved OB (oligonucleotide/oligosaccharide binding) fold. This ssDNA-binding domain was presumably present in the common ancestor to all three major branches of life. In recent years, there has been an increasing interest in SSBs because they are useful for molecular biology methods and for analytical purposes. In this review, we concentrate on recent advances in the discovery of new sources of SSBs as well as certain aspects of their applications in analytical sciences.
    Źródło:
    Acta Biochimica Polonica; 2005, 52, 3; 569-574
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-4 z 4

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