Purification of fusion protein HSA/IL1ra and its bioactivity.

Author: Qi SHEN ¹ ; Shu-Qing CHEN
Author Information

1. Institute of Pharmacology, Toxicology and Biological Pharmaceutics, College of Pharmaceutical Sciences, Zhejiang University, Hangzhou 310058, China.
Publication Type:Journal Article
MeSH: Apoptosis; drug effects; Cell Line, Tumor; Humans; Interleukin 1 Receptor Antagonist Protein; biosynthesis; genetics; Melanoma; pathology; Pichia; genetics; metabolism; Recombinant Fusion Proteins; biosynthesis; genetics; isolation & purification; pharmacology; Serum Albumin; biosynthesis; genetics
From: Journal of Zhejiang University. Medical sciences 2009;38(3):260-264
CountryChina
Language:Chinese
Abstract:
OBJECTIVETo purify the recombinant human serum albumin fusion protein with interleukin 1 (HAS/IL1ra) and to detect the bioactivity of the fusion protein.
METHODSThe 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.
RESULTThe 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.
CONCLUSIONThe purified recombinant HAS/IL1ra protein in this study has a satisfactory bioactivity.