Preparation of N2, N2,7-trimethylguanosine affinity columns

Nucleosides Nucleotides. 1999 Jan;18(1):125-36. doi: 10.1080/07328319908045599.

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

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antibodies
  • Antibodies, Monoclonal
  • Carrier Proteins / isolation & purification*
  • Cell Nucleus / chemistry
  • Chromatography, Affinity / instrumentation
  • Chromatography, Affinity / methods*
  • Cytoplasm / chemistry
  • Fungal Proteins / isolation & purification
  • Guanosine / analogs & derivatives*
  • Guanosine / chemical synthesis
  • HeLa Cells
  • Hemocyanins
  • Humans
  • Mice
  • Nuclear Proteins / isolation & purification*
  • Rabbits
  • Saccharomyces cerevisiae
  • Sepharose
  • Serum Albumin

Substances

  • Antibodies
  • Antibodies, Monoclonal
  • Carrier Proteins
  • Fungal Proteins
  • Nuclear Proteins
  • Serum Albumin
  • Guanosine
  • N(2),N(2),7-trimethylguanosine
  • Sepharose
  • Hemocyanins
  • keyhole-limpet hemocyanin