A novel application of ion exchange chromatography in recombinant hepatitis B vaccine downstream processing: Improving recombinant HBsAg homogeneity by removing associated aggregates
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Clinical Biochemistry,Biochemistry,General Medicine,Analytical Chemistry
Reference55 articles.
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2. Characterization of the lipid and protein organization in HBsAg viral particles by steady-state and time-resolved fluorescence spectroscopy;Greiner;Biochimie,2010
3. A highly efficient hydrophobic interaction chromatographic absorbent improved the purification of hepatitis B surface antigen (HBsAg) derived from Hansenula polymorpha cell;Zhou;Process Biochem.,2007
4. Expression, purification, and characterization of hepatitis B virus surface antigens (HBsAg) in yeast Pichia pastoris;Liu;Appl. Biochem. Biotechnol.,2009
5. Extraction and purification of hepatitis B virus-like M particles from a recombinant Saccharomyces cerevisiae strain using alumina powder;Hadiji-Abbes;J. Virol. Methods,2013
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