Purification of fusion protein HSA/IL1ra and its bioactivity / 浙江大学学报·医学版
Journal of Zhejiang University. Medical sciences
; (6): 260-264, 2009.
Article
in Zh
| WPRIM
| ID: wpr-310357
Responsible library:
WPRO
ABSTRACT
<p><b>OBJECTIVE</b>To purify the recombinant human serum albumin fusion protein with interleukin 1 (HAS/IL1ra) and to detect the bioactivity of the fusion protein.</p><p><b>METHODS</b>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.</p><p><b>RESULT</b>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.</p><p><b>CONCLUSION</b>The purified recombinant HAS/IL1ra protein in this study has a satisfactory bioactivity.</p>
Full text:
1
Index:
WPRIM
Main subject:
Pathology
/
Pharmacology
/
Pichia
/
Recombinant Fusion Proteins
/
Serum Albumin
/
Apoptosis
/
Cell Line, Tumor
/
Interleukin 1 Receptor Antagonist Protein
/
Genetics
/
Melanoma
Limits:
Humans
Language:
Zh
Journal:
Journal of Zhejiang University. Medical sciences
Year:
2009
Type:
Article