title: [Purification of fusion protein HSA/IL1ra and its bioactivity].
abstract: To purify the recombinant human serum albumin fusion protein with interleukin 1 (HAS/IL1ra) and to detect the bioactivity of the fusion protein.
  
  
  
  The recombinant HAS/IL1ra protein was purified by affinity chromatography and ion exchange chromatography, the bioactivity of the fusion protein was detected by IL1-induced A375 S2 cell killing.
  
  
  
  The purity of the fusion protein was at least 98 % as assessed by HPLC and the protective effect from the IL1-induced A375 S2 cell killing was similar to natural IL1ra.
  
  
  
  The purified recombinant HAS/IL1ra protein in this study has a satisfactory bioactivity.
authors.affiliation: Institute of Pharmacology, Toxicology and Biological Pharmaceutics, College of Pharmaceutical Sciences, Zhejiang University, Hangzhou 310058, China.
authors.forename: Qi
authors.initials: Q
authors.lastname: Shen
authors.forename: Shu-Qing
authors.initials: SQ
authors.lastname: Chen
mesh_terms: D017209:Apoptosis / Q000187:drug effects; D045744:Cell Line, Tumor; D006801:Humans; D053590:Interleukin 1 Receptor Antagonist Protein / Q000096:biosynthesis* / Q000235:genetics; D008545:Melanoma / Q000473:pathology; D010843:Pichia / Q000235:genetics / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis / Q000235:genetics / Q000302:isolation & purification* / Q000494:pharmacology*; D012709:Serum Albumin / Q000096:biosynthesis* / Q000235:genetics
chemical_list: D053590:Interleukin 1 Receptor Antagonist Protein; D011993:Recombinant Fusion Proteins; D012709:Serum Albumin