Affinity purification of recombinant cholera toxin B subunit oligomer expressed in Bacillus brevis for potential human use as a mucosal adjuvant.
Identifieur interne : 002685 ( PubMed/Curation ); précédent : 002684; suivant : 002686Affinity purification of recombinant cholera toxin B subunit oligomer expressed in Bacillus brevis for potential human use as a mucosal adjuvant.
Auteurs : Y. Yasuda [Japon] ; K. Matano ; T. Asai ; K. TochikuboSource :
- FEMS immunology and medical microbiology [ 0928-8244 ] ; 1998.
Descripteurs français
- KwdFr :
- Adjuvants immunologiques (), Adjuvants immunologiques (isolement et purification), Bacillus (métabolisme), Chromatographie d'affinité (), Coloration à l'argent, Humains, Protéines recombinantes (), Protéines recombinantes (isolement et purification), Test ELISA, Toxine cholérique (), Toxine cholérique (isolement et purification), Électrophorèse sur gel de polyacrylamide.
- MESH :
- isolement et purification : Adjuvants immunologiques, Protéines recombinantes, Toxine cholérique.
- métabolisme : Bacillus.
- Adjuvants immunologiques, Chromatographie d'affinité, Coloration à l'argent, Humains, Protéines recombinantes, Test ELISA, Toxine cholérique, Électrophorèse sur gel de polyacrylamide.
English descriptors
- KwdEn :
- Adjuvants, Immunologic (chemistry), Adjuvants, Immunologic (isolation & purification), Bacillus (metabolism), Cholera Toxin (chemistry), Cholera Toxin (isolation & purification), Chromatography, Affinity (methods), Electrophoresis, Polyacrylamide Gel, Enzyme-Linked Immunosorbent Assay, Humans, Recombinant Proteins (chemistry), Recombinant Proteins (isolation & purification), Silver Staining.
- MESH :
- chemical , chemistry : Adjuvants, Immunologic, Cholera Toxin, Recombinant Proteins.
- chemical , isolation & purification : Adjuvants, Immunologic, Cholera Toxin, Recombinant Proteins.
- metabolism : Bacillus.
- methods : Chromatography, Affinity.
- Electrophoresis, Polyacrylamide Gel, Enzyme-Linked Immunosorbent Assay, Humans, Silver Staining.
Abstract
For use as a mucosal adjuvant for human vaccines, a simple method has been developed for the affinity purification of recombinant cholera toxin B subunit which had been expressed in a safe host, Bacillus brevis. Recombinant cholera toxin B subunit, adsorbed quantitatively to a D-galactose-agarose column, was eluted with an 0.1-0.4 M D-galactose gradient with a yield of > 90%. The cholera toxin B subunit preparation was similar to the native cholera toxin B subunit with respect to GM1 binding ability, remarkable stability of the pentamer, and the dissociation-reassociation property by shifting pHs. Cross-linking experiments with glutaraldehyde demonstrated that the pentameric form was predominant; tetrameric, trimeric, dimeric and monomeric forms were detected to a lesser extent, and additionally 10- and 15-mers were observed depending on the concentration of the cholera toxin B subunit.
DOI: 10.1111/j.1574-695X.1998.tb01141.x
PubMed: 9626936
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pubmed:9626936Le document en format XML
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Recombinant cholera toxin B subunit, adsorbed quantitatively to a D-galactose-agarose column, was eluted with an 0.1-0.4 M D-galactose gradient with a yield of > 90%. The cholera toxin B subunit preparation was similar to the native cholera toxin B subunit with respect to GM1 binding ability, remarkable stability of the pentamer, and the dissociation-reassociation property by shifting pHs. Cross-linking experiments with glutaraldehyde demonstrated that the pentameric form was predominant; tetrameric, trimeric, dimeric and monomeric forms were detected to a lesser extent, and additionally 10- and 15-mers were observed depending on the concentration of the cholera toxin B subunit.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">9626936</PMID><DateCompleted><Year>1998</Year><Month>08</Month><Day>06</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>30</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0928-8244</ISSN><JournalIssue CitedMedium="Print"><Volume>20</Volume><Issue>4</Issue><PubDate><Year>1998</Year><Month>Apr</Month></PubDate></JournalIssue><Title>FEMS immunology and medical microbiology</Title><ISOAbbreviation>FEMS Immunol. Med. Microbiol.</ISOAbbreviation></Journal><ArticleTitle>Affinity purification of recombinant cholera toxin B subunit oligomer expressed in Bacillus brevis for potential human use as a mucosal adjuvant.</ArticleTitle><Pagination><MedlinePgn>311-8</MedlinePgn></Pagination><Abstract><AbstractText>For use as a mucosal adjuvant for human vaccines, a simple method has been developed for the affinity purification of recombinant cholera toxin B subunit which had been expressed in a safe host, Bacillus brevis. Recombinant cholera toxin B subunit, adsorbed quantitatively to a D-galactose-agarose column, was eluted with an 0.1-0.4 M D-galactose gradient with a yield of > 90%. The cholera toxin B subunit preparation was similar to the native cholera toxin B subunit with respect to GM1 binding ability, remarkable stability of the pentamer, and the dissociation-reassociation property by shifting pHs. Cross-linking experiments with glutaraldehyde demonstrated that the pentameric form was predominant; tetrameric, trimeric, dimeric and monomeric forms were detected to a lesser extent, and additionally 10- and 15-mers were observed depending on the concentration of the cholera toxin B subunit.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Yasuda</LastName><ForeName>Y</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Department of Microbiology, Nagoya City University Medical School, Nagoya, Japan. yyasuda@med.nagoya-cu.ac.jp</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Matano</LastName><ForeName>K</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Asai</LastName><ForeName>T</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Tochikubo</LastName><ForeName>K</ForeName><Initials>K</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>FEMS Immunol Med Microbiol</MedlineTA><NlmUniqueID>9315554</NlmUniqueID><ISSNLinking>0928-8244</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000276">Adjuvants, Immunologic</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>9012-63-9</RegistryNumber><NameOfSubstance UI="D002772">Cholera Toxin</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000276" MajorTopicYN="N">Adjuvants, Immunologic</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000302" MajorTopicYN="Y">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001407" MajorTopicYN="N">Bacillus</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002772" MajorTopicYN="N">Cholera Toxin</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000302" MajorTopicYN="Y">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002846" MajorTopicYN="N">Chromatography, Affinity</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="N">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004591" MajorTopicYN="N">Electrophoresis, Polyacrylamide Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004797" MajorTopicYN="N">Enzyme-Linked Immunosorbent Assay</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016622" MajorTopicYN="N">Silver Staining</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1998</Year><Month>6</Month><Day>17</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1998</Year><Month>6</Month><Day>17</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1998</Year><Month>6</Month><Day>17</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">9626936</ArticleId><ArticleId IdType="pii">S0928-8244(98)00027-3</ArticleId><ArticleId IdType="doi">10.1111/j.1574-695X.1998.tb01141.x</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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