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Purification of fusion protein HSA/IL1ra and its bioactivity / 浙江大学学报·医学版
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>
Subject(s)
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
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