Publicação: Preparation of N2, N2,7-trimethylguanosine affinity columns
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2,2,7-trimethylguanosine (TMG) binding proteins from human cells were purified through TMG-affinity columns. TMG synthesis was improved and the TMG obtained was shown to be similar to the TMG in the 5' cap of the UsnRNAs. The eluates obtained with TMG-affinity chromatographies were very different from those isolated with m7G-affinity columns, thus suggesting that specific TMG- binding proteins were obtained. The fraction may be enriched with factors associated with import and/or hypermethylation of UsnRNPs.
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binding protein, guanosine derivative, small nuclear RNA, antibody, carrier protein, drug derivative, fungal protein, guanosine, hemocyanin, keyhole limpet hemocyanin, keyhole-limpet hemocyanin, monoclonal antibody, N(2),N(2),7 trimethylguanosine, N(2),N(2),7-trimethylguanosine, nuclear protein, sepharose, serum albumin, affinity chromatography, animal experiment, extraction, human, mouse, nonhuman, nucleotide metabolism, protein methylation, protein purification, spliceosome, synthesis, animal, cell nucleus, chemistry, cytoplasm, HeLa cell, instrumentation, isolation and purification, methodology, rabbit, Saccharomyces cerevisiae, Animals, Antibodies, Antibodies, Monoclonal, Carrier Proteins, Cell Nucleus, Chromatography, Affinity, Cytoplasm, Fungal Proteins, Guanosine, Hela Cells, Hemocyanin, Humans, Mice, Nuclear Proteins, Rabbits, Sepharose, Serum Albumin
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Nucleosides and Nucleotides, v. 18, n. 1, p. 125-136, 1999.
