Purification and point-mutation analysis of human interleukin-2 (Ser-125)

Chin J Biotechnol. 1992;8(4):219-25.

Abstract

A new type of IL-2(Ser-125) was purified by semi-preparative RP-HPLC, and its purity was analyzed with microbore HPLC, IEF, SDS-PAGE and capillary electrophoresis (CE). The N-terminal sequencing indicated the microheterogeneity of the N-terminus, i.e., N-Met(2/3) and N-Ala(1/3), which was identified with the results of CE and IEF. The amino acid sequence of the point mutated peptide confirmed the replacement of Cys-125 with Ser.

MeSH terms

  • Amino Acid Sequence
  • Chromatography, High Pressure Liquid
  • Electrophoresis, Polyacrylamide Gel
  • Humans
  • Interleukin-2 / genetics*
  • Interleukin-2 / isolation & purification
  • Isoelectric Focusing
  • Molecular Sequence Data
  • Peptide Mapping
  • Point Mutation*
  • Serine / genetics*

Substances

  • Interleukin-2
  • Serine