Title : Structure of recombinant human
interleukin 5 produced by Chinese hamster ovary cells
Abstract :
- 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
- Each peptide fragment generated by Achromobacter protease I (API) digestion was purified and characterized by amino acid analysis and amino acid sequence analysis
- After digestion with API, we could identify all the peptides which were expected from human IL-5 cDNA sequence
- 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
- In addition, we concluded that Thr-3 and Asn-28 were glycosylated
- 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
Output (sent_index, trigger,
protein,
sugar,
site):
- 1. glycosylation, , -, -, sites
- 5. glycosylated, , -, -, Thr-3 and Asn-28
Output(Part-Of) (sent_index,
protein,
site):
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):
- 5. interleukin 5, -, Thr-3 and Asn-28