Characterization of recombinant human interleukin-2 with micromethods

J Chromatogr. 1985 Jun 19;326:357-61. doi: 10.1016/s0021-9673(01)87461-6.


Highly purified recombinant human interleukin-2, expressed in Escherichia coli, was analyzed by micromethods. N-Terminal sequence analysis showed that methionine at position 0 was found in 90% of the molecules and not completely removed in post-ribosomal processing. A complete peptide map of the reduced and S-carboxymethylated protein was obtained by high-performance liquid chromatography after tryptic digestion, and the fragments were identified by amino acid analysis and automated Edman sequence analysis. Using a double-label S-carboxymethylation procedure, it was determined that there is a disulfide linkage between the cysteine residues at positions 58 and 105. The third cysteine residue at position 125 was found to be present as the free sulfhydryl.

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / analysis
  • Chromatography, High Pressure Liquid
  • DNA, Recombinant*
  • Humans
  • Hydrolysis
  • Interleukin-2 / analysis*
  • Interleukin-2 / genetics
  • Microchemistry
  • Peptide Fragments / analysis
  • Trypsin


  • Amino Acids
  • DNA, Recombinant
  • Interleukin-2
  • Peptide Fragments
  • Trypsin