Analysis and characterization of hepatitis B vaccine particles synthesized from Hansenula polymorpha
DC Field | Value | Language |
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dc.contributor.author | Seo, Hyuk-Seong | - |
dc.contributor.author | Park, Jin-Seung | - |
dc.contributor.author | Han, Kyung-Yeon | - |
dc.contributor.author | Bae, Kyung-Dong | - |
dc.contributor.author | Ahn, Sang Jeorn | - |
dc.contributor.author | Kang, Hyun Ah | - |
dc.contributor.author | Lee, Jeewon | - |
dc.date.accessioned | 2021-09-09T05:21:40Z | - |
dc.date.available | 2021-09-09T05:21:40Z | - |
dc.date.created | 2021-06-10 | - |
dc.date.issued | 2008-08-05 | - |
dc.identifier.issn | 0264-410X | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/122874 | - |
dc.description.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. (C) 2008 Elsevier Ltd. All rights reserved, | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | ELSEVIER SCI LTD | - |
dc.subject | SURFACE-ANTIGEN | - |
dc.subject | HIGH-AFFINITY | - |
dc.subject | PROTEIN | - |
dc.subject | VIRUS | - |
dc.subject | YEAST | - |
dc.subject | IMMUNOGENICITY | - |
dc.subject | GLYCOSYLATION | - |
dc.subject | LECTIN | - |
dc.subject | STABILITY | - |
dc.subject | CELLS | - |
dc.title | Analysis and characterization of hepatitis B vaccine particles synthesized from Hansenula polymorpha | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Lee, Jeewon | - |
dc.identifier.doi | 10.1016/j.vaccine.2008.05.070 | - |
dc.identifier.scopusid | 2-s2.0-47149115664 | - |
dc.identifier.wosid | 000258522800007 | - |
dc.identifier.bibliographicCitation | VACCINE, v.26, no.33, pp.4138 - 4144 | - |
dc.relation.isPartOf | VACCINE | - |
dc.citation.title | VACCINE | - |
dc.citation.volume | 26 | - |
dc.citation.number | 33 | - |
dc.citation.startPage | 4138 | - |
dc.citation.endPage | 4144 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Immunology | - |
dc.relation.journalResearchArea | Research & Experimental Medicine | - |
dc.relation.journalWebOfScienceCategory | Immunology | - |
dc.relation.journalWebOfScienceCategory | Medicine, Research & Experimental | - |
dc.subject.keywordPlus | SURFACE-ANTIGEN | - |
dc.subject.keywordPlus | HIGH-AFFINITY | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordPlus | VIRUS | - |
dc.subject.keywordPlus | YEAST | - |
dc.subject.keywordPlus | IMMUNOGENICITY | - |
dc.subject.keywordPlus | GLYCOSYLATION | - |
dc.subject.keywordPlus | LECTIN | - |
dc.subject.keywordPlus | STABILITY | - |
dc.subject.keywordPlus | CELLS | - |
dc.subject.keywordAuthor | hepatitis B surface antigen | - |
dc.subject.keywordAuthor | yeast | - |
dc.subject.keywordAuthor | covalent multimer | - |
dc.subject.keywordAuthor | glycosylation | - |
dc.subject.keywordAuthor | stability | - |
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