Preparation of N2, N2,7-trimethylguanosine affinity columns
Contribuinte(s) |
Universidade Estadual Paulista (UNESP) |
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Data(s) |
27/05/2014
27/05/2014
01/01/1999
|
Resumo |
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. |
Formato |
125-136 |
Identificador |
http://dx.doi.org/10.1080/07328319908045599 Nucleosides and Nucleotides, v. 18, n. 1, p. 125-136, 1999. 0732-8311 http://hdl.handle.net/11449/65686 10.1080/07328319908045599 2-s2.0-0032589080 |
Idioma(s) |
eng |
Relação |
Nucleosides and Nucleotides |
Direitos |
closedAccess |
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 |
Tipo |
info:eu-repo/semantics/article |