PMID: 2361960

 

    Legend: Sugar

Title : Structure of recombinant human interleukin 5 produced by Chinese hamster ovary cells

Abstract :
  1. The complete peptide map of purified recombinant human interleukin 5 ( rhIL-5 ) was determined to verify its primary structure, glycosylation sites , and disulfide bonding structure
  2. Each peptide fragment generated by Achromobacter protease I (API) digestion was purified and characterized by amino acid analysis and amino acid sequence analysis
  3. After digestion with API, we could identify all the peptides which were expected from human IL-5 cDNA sequence
  4. The analyses of sulfhydryl content in rhIL-5 molecule and disulfide-containing peptide obtained from API digestion indicated that active form of rhIL-5 existed as an antiparallel dimer linked by two pairs of Cys-44 and Cys-86
  5. In addition, we concluded that Thr-3 and Asn-28 were glycosylated
  6. The results indicate that primary structure of rhIL-5 is highly homogeneous and observed heterogeneity is due to the difference in the content of carbohydrate