exo-n-(2-(4-azidotetrafluorobenzamido)ethyl)-deoxycytidine-5--triphosphate and 2--deoxycytidine-5--triphosphate

exo-n-(2-(4-azidotetrafluorobenzamido)ethyl)-deoxycytidine-5--triphosphate has been researched along with 2--deoxycytidine-5--triphosphate* in 2 studies

Other Studies

2 other study(ies) available for exo-n-(2-(4-azidotetrafluorobenzamido)ethyl)-deoxycytidine-5--triphosphate and 2--deoxycytidine-5--triphosphate

ArticleYear
Photoaffinity labeling of DNA polymerase from Thermus thermophilus and DNA template by photoreactive analogs of dCTP.
    Biochemistry. Biokhimiia, 1998, Volume: 63, Issue:8

    Substrate properties of dCTP analogs N4-[2-(4-azidotetrafluorobenzoylamino)-ethyl]-2;-deoxycytidine-5; -triphosphate (FABdCTP), 5-[N-(4-azidotetrafluorobenzoyl)-3-amino-trans-propen-1-yl] -2;-deoxycytidine-5;-triphosphate (AlFABdCTP), and N4-[2-(2-nitro-5-azidobenzoylamino)-ethyl]-2;-deoxycytidine-5; -triphosphate (NABdCTP) were studied in the reaction of DNA synthesis catalyzed by DNA polymerase from the extremely thermophilic bacterium Thermus thermophilus B 35 (Tte DNA polymerase). The enzyme was photoaffinity labeled with the mentioned derivatives, NABdCTP being used for the first time. The photoreactive primers containing FABdCTP and AlFABdCTP were synthesized in situ by Tte DNA polymerase and used in the complementary addressed labeling of DNA template. The efficiency of DNA template labeling is shown to be a function of the structure of the photoactive group.

    Topics: Affinity Labels; Azides; Base Sequence; Catalysis; Deoxycytosine Nucleotides; DNA Primers; DNA-Directed DNA Polymerase; Phosphorus; Photolysis; Templates, Genetic; Thermus thermophilus

1998
Affinity modification of human immunodeficiency virus reverse transcriptase and DNA template by photoreactive dCTP analogs.
    FEBS letters, 1994, Nov-07, Volume: 354, Issue:2

    New base-substituted analogs of dCTP containing an azido group have been synthesized and applied to a selective photoaffinity modification of HIV-RT (p66/p51 heterodimer). The labeling of only the 66 kDa subunit of HIV-RT was detected when the enzyme was first irradiated with the analogs and then template (5'-(d)GGTTAAATAAAATAGTAAGAATGTATAGCCCCTACCA-3') and 5' 32P end-labeled 3'-(d)TTACATATCGGGGATGGT-5' primer were added. The 5' 32P end-labeled primer elongated by dCTP analogs in the presence of both HIV-RT and DNA template is able to modify both subunits of HIV-RT and DNA template. This way of specific cross-linking to both DNA (RNA) template and HIV-RT opens up new possibilities to study the HIV-RT active site.

    Topics: Affinity Labels; Base Sequence; Binding Sites; Deoxycytosine Nucleotides; DNA; HIV; Molecular Sequence Data; Molecular Structure; Photochemistry; RNA-Directed DNA Polymerase; Templates, Genetic; Ultraviolet Rays

1994