Abstract
The biochemical and physical properties of hepatitis B virus (HBV) small surface antigen (S-HBVsAg) from Berna Biotech Korea Corp. were systematically analyzed and characterized. Through various electrophoresis and immunoblotting assay of S-HBVsAg and its proteolytic products, it was confirmed that the S-HBVsAg vaccine particles are present in the form of covalent multimers that are assembled via strong intermolecular disulfide bonds. The S-HBVsAg particles contain no N-glycosylation moiety but some O-glycosidically linked mannoses. Evidently from N-terminus sequencing of both monomers and dimers that are formed by complete and partial reduction, respectively, of the S-HBVsAg particles under reducing SDS-PAGE condition, it is evident that each polypeptide within S-HBVsAg particles has authentic sequence of N-terminus. Denaturation plot shows that the S-HBVsAg vaccine particles were extremely stable especially in the solution with high acidity. This stability property of S-HBVsAg vaccine particles could provide very useful information for the optimization of the downstream process of recombinant S-HBVsAg particles synthesized from yeast cultures.
Original language | English |
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Pages (from-to) | 4138-4144 |
Number of pages | 7 |
Journal | Vaccine |
Volume | 26 |
Issue number | 33 |
DOIs | |
Publication status | Published - 2008 Aug 5 |
Keywords
- Covalent multimer
- Glycosylation
- Hepatitis B surface antigen
- Stability
- Yeast
ASJC Scopus subject areas
- Molecular Medicine
- Immunology and Microbiology(all)
- veterinary(all)
- Public Health, Environmental and Occupational Health
- Infectious Diseases