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Sensitized photomodification of oligonucleotide-binding proteins displayed on the eucaryotic cell surface
Authors:T I Gainutdinov  O E Shestova  L A Yakubov  M I Dobrikov  V V Vlassov
Institution:(1) Novosibirsk Institute of Bioorganic Chemistry, 8 prosp. Akad. Lavrent"eva, 630090 Novosibirsk, Russian Federation
Abstract:Interactions of double-stranded nucleic acids with cell surface proteins, which are involved in binding and transport of extracellular nucleic acids, were studied by the photoaffinity modification with a binary system of oligonucleotide conjugates. The photoreactive double-stranded complex involved an oligonucleotide template and two complementary to adjacent sequences oligonucleotide conjugates. One conjugate contained a photoreagent, viz., 4-azido-2,3,5,6-tetrafluorobenzaldehyde N-(3-aminopropionyl)hydrazone, at the terminus located in proximity to the terminus of another conjugate containing the sensitizer, viz., 9-aminomethylanthracene. Binding of photoreagent and the sensitizer to a single-stranded template yields the photoreactive center. Upon irradiation with visible light (400—580 nm), this photoreactive double-stranded complex forms covalent cross-linkages with oligonucleotide-binding surface proteins of eucaryotic SPEV cells.
Keywords:oligonucleotide-binding proteins  sensitized photomodification of proteins  4-azido-2  3  5  6-tetrafluorobenzaldehyde N-(3-aminopropionyl)hydrazone  9-aminomethylanthracene
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