Expression in Pichia pastoris and properties of human serum albumin-interferon alpha2b chimera / 生物工程学报
Chinese Journal of Biotechnology
;
(12): 173-179, 2006.
Article
in Chinese
| WPRIM
| ID: wpr-237005
ABSTRACT
To reduce the serum clearance of interferon alpha2b, a chimeric gene encoding an human serum albumin(HSA)--human interferon alpha2b(IFNalpha2b) fusion protein was overexpressed in Pichia pastoris. After fermentation in a 5L bioreactor, the fusion protein, capable of cross-reacting with anti-IFN alpha and anti-HSA antibody, was purified from the culture of the recombinant yeast by ultrafiltration, blue Sepharose affinity, phenyl hydrophobic interaction and Q ion exchange chromatography. Its IFNa2b moiety exhibits antiviral activity similar to that of recombinant human IFNa2b. In Cynomolgus monkeys model, The fusion protein was detectable in plasma, even 336h after a single does of 90 microg/kg injection intravenously or subcutaneously. The elimination phase half-life of the fusion protein was 101h after intravenous injection and 68.2h after subcutaneous injection. Its Subcutaneous bioavailability was 67.9%. The enhanced pharmacokinetics of interferon a2b fused to human serum albumin suggest its promissing application in clinic medicine.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Pichia
/
Recombinant Fusion Proteins
/
Recombinant Proteins
/
Serum Albumin
/
Pharmacokinetics
/
Interferon-alpha
/
Bioreactors
/
Fermentation
/
Genetics
/
Macaca fascicularis
Limits:
Animals
/
Humans
Language:
Chinese
Journal:
Chinese Journal of Biotechnology
Year:
2006
Type:
Article
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