| pH-dependent aggregation and secretion of soluble monomeric influenza hemagglutinin. | |
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MedLine Citation:
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PMID: 9541609 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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We previously reported the expression of soluble A/Victoria/3/75 (H3N2) hemagglutinin in insect cells and the molecular and immunological structure of an aggregated fraction, only observed in cell supernatant when expression was performed at low pH [23]. Here we report that besides this aggregated a monomeric and possibly a trimeric structure is detected in cell supernatant, irrespective of the pH of the medium. Evidence is presented that the aggregated fraction is generated out of monomeric HAOs molecules due to a low intracellular pH encountered during secretion. |
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Authors:
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P Vanlandschoot; E Beirnaert; J Grooten; W M Jou; W Fiers |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Archives of virology Volume: 143 ISSN: 0304-8608 ISO Abbreviation: Arch. Virol. Publication Date: 1998 |
Date Detail:
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Created Date: 1998-04-23 Completed Date: 1998-04-23 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 7506870 Medline TA: Arch Virol Country: AUSTRIA |
Other Details:
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Languages: eng Pagination: 227-39 Citation Subset: IM |
Affiliation:
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Laboratory of Molecular Biology, Flanders Interuniversity Institute of Biotechnology, University of Ghent, Belgium. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Antibodies, Monoclonal / immunology Cell Line Hemagglutinin Glycoproteins, Influenza Virus / chemistry*, metabolism Hydrogen-Ion Concentration Protein Folding Recombinant Proteins / chemistry Spodoptera |
| Chemical | |
Reg. No./Substance:
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0/Antibodies, Monoclonal; 0/Hemagglutinin Glycoproteins, Influenza Virus; 0/Recombinant Proteins |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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