Dissociation of recombinant tumor necrosis factor-alpha studied by gel permeation chromatography

Biochem Biophys Res Commun. 1987 Sep 15;147(2):740-6. doi: 10.1016/0006-291x(87)90992-2.


The structure of tumor necrosis factor-alpha (TNF-alpha) was studied using gel permeation chromatography. At an initial protein concentration of 0.4 mg/ml, the TNF-alpha exists as a compact trimer with a Stokes radius of 2.3 +/- 0.1 nm. This trimer dissociates as the protein concentration is decreased, and this dissociation is effected by pH. At the lower protein concentrations at pH 6.0 a species with a Stokes radius of 1.9 +/- 0.1 nm, possibly monomer, is evident. This species is not obvious at pH 7.0, but instead a species with a Stokes radius of 2.2 +/- 0.1 nm appears.

MeSH terms

  • Chemical Phenomena
  • Chemistry, Physical
  • Chromatography, High Pressure Liquid
  • Glycoproteins / isolation & purification*
  • Hydrogen-Ion Concentration
  • Macromolecular Substances
  • Molecular Weight
  • Recombinant Proteins / isolation & purification*
  • Solutions
  • Tumor Necrosis Factor-alpha


  • Glycoproteins
  • Macromolecular Substances
  • Recombinant Proteins
  • Solutions
  • Tumor Necrosis Factor-alpha