Preparation of N2, N2,7-trimethylguanosine affinity columns
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Taylor & Francis
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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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Palavras-chave
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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Inglês
Citação
Nucleosides and Nucleotides, v. 18, n. 1, p. 125-136, 1999.
