Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Antibodies
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Antibodies, Monoclonal
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Carrier Proteins / isolation & purification*
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Cell Nucleus / chemistry
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Chromatography, Affinity / instrumentation
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Chromatography, Affinity / methods*
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Cytoplasm / chemistry
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Fungal Proteins / isolation & purification
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Guanosine / analogs & derivatives*
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Guanosine / chemical synthesis
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HeLa Cells
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Hemocyanins
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Humans
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Mice
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Nuclear Proteins / isolation & purification*
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Rabbits
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Saccharomyces cerevisiae
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Sepharose
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Serum Albumin
Substances
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Antibodies
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Antibodies, Monoclonal
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Carrier Proteins
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Fungal Proteins
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Nuclear Proteins
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Serum Albumin
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Guanosine
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N(2),N(2),7-trimethylguanosine
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Sepharose
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Hemocyanins
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keyhole-limpet hemocyanin