Sequential affinity purification of peroxidase tagged bispecific anti-SARS-CoV antibodies on phenylboronic acid agarose.
Identifieur interne : 001B78 ( Ncbi/Merge ); précédent : 001B77; suivant : 001B79Sequential affinity purification of peroxidase tagged bispecific anti-SARS-CoV antibodies on phenylboronic acid agarose.
Auteurs : Pravin K. Bhatnagar [Canada] ; Dipankar Das ; Mavanur R. SureshSource :
- Journal of chromatography. B, Analytical technologies in the biomedical and life sciences [ 1570-0232 ] ; 2008.
Descripteurs français
- KwdFr :
- Affinité des anticorps, Agarose (), Agarose (analogues et dérivés), Animaux, Anticorps antiviraux (isolement et purification), Anticorps bispécifiques (isolement et purification), Anticorps monoclonaux (immunologie), Anticorps monoclonaux (isolement et purification), Chromatographie d'affinité (), Horseradish peroxidase (), Hybridomes (immunologie), Rats, Sites de fixation des anticorps, Techniques immunoenzymatiques, Test ELISA (), Virus du SRAS (immunologie).
- MESH :
- analogues et dérivés : Agarose.
- immunologie : Anticorps monoclonaux, Hybridomes, Virus du SRAS.
- isolement et purification : Anticorps antiviraux, Anticorps bispécifiques, Anticorps monoclonaux.
- Affinité des anticorps, Agarose, Animaux, Chromatographie d'affinité, Horseradish peroxidase, Rats, Sites de fixation des anticorps, Techniques immunoenzymatiques, Test ELISA.
English descriptors
- KwdEn :
- Animals, Antibodies, Bispecific (isolation & purification), Antibodies, Monoclonal (immunology), Antibodies, Monoclonal (isolation & purification), Antibodies, Viral (isolation & purification), Antibody Affinity, Binding Sites, Antibody, Chromatography, Affinity (methods), Enzyme-Linked Immunosorbent Assay (methods), Horseradish Peroxidase (chemistry), Hybridomas (immunology), Immunoenzyme Techniques, Rats, SARS Virus (immunology), Sepharose (analogs & derivatives), Sepharose (chemistry).
- MESH :
- chemical , analogs & derivatives : Sepharose.
- chemical , chemistry : Horseradish Peroxidase, Sepharose.
- chemical , immunology : Antibodies, Monoclonal.
- chemical , isolation & purification : Antibodies, Bispecific, Antibodies, Monoclonal, Antibodies, Viral.
- immunology : Hybridomas, SARS Virus.
- methods : Chromatography, Affinity, Enzyme-Linked Immunosorbent Assay.
- Animals, Antibody Affinity, Binding Sites, Antibody, Immunoenzyme Techniques, Rats.
Abstract
Hybrid hybridomas (quadromas) are derived by fusing at least two hybridomas, each producing a different antibody of predefined specificity. The resulting cell secretes not only the immunoglobulins of both parents but also hybrid molecules manifesting the binding characteristics of the individual fusion partners. Purification of the desired bispecific immunoprobe with high specific activity from a mixture of bispecific and monospecific monoclonal antibodies requires special strategies. Using a dual, sequential affinity chromatography (Protein-G chromatography followed by m-aminophenyleboronic acid agarose column), we have purified bispecific monoclonal antibodies (BsMAb) as a preformed HRPO (Horseradish Peroxidase) complex (BsMAb-HRPO). The quadroma culture supernatant was initially processed on a Protein-G column to isolate all the species of immunoglobulins. This pre-enriched fraction was subsequently passed through the aminophenyleboronic acid column super saturated with HRPO. The column matrix has the ability to bind to proteins such as HRPO with vicinal diols. The enzyme loaded column captures the desired bispecific anti-SARS-CoVxanti-HRPO species with the elimination of the monospecific anti-SARS-CoV MAb to result in a high specific activity diagnostic probe. The presence of anti-HRPO MAb is an acceptable impurity as it will not bind to the target SARS-CoV NP antigen and will get washed out during the ELISA procedure.
DOI: 10.1016/j.jchromb.2008.01.003
PubMed: 18258500
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Bhatnagar</name><affiliation wicri:level="1"><nlm:affiliation>Faculty of Pharmacy and Pharmaceutical Sciences, University of Alberta, Edmonton, Alberta, Canada T6G 2N8.</nlm:affiliation><country>Canada</country><wicri:regionArea>Faculty of Pharmacy and Pharmaceutical Sciences, University of Alberta, Edmonton, Alberta</wicri:regionArea><wicri:noRegion>Alberta</wicri:noRegion></affiliation></author><author><name sortKey="Das, Dipankar" sort="Das, Dipankar" uniqKey="Das D" first="Dipankar" last="Das">Dipankar Das</name></author><author><name sortKey="Suresh, Mavanur R" sort="Suresh, Mavanur R" uniqKey="Suresh M" first="Mavanur R" last="Suresh">Mavanur R. Suresh</name></author></analytic><series><title level="j">Journal of chromatography. B, Analytical technologies in the biomedical and life sciences</title><idno type="ISSN">1570-0232</idno><imprint><date when="2008" type="published">2008</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Antibodies, Bispecific (isolation & purification)</term><term>Antibodies, Monoclonal (immunology)</term><term>Antibodies, Monoclonal (isolation & purification)</term><term>Antibodies, Viral (isolation & purification)</term><term>Antibody Affinity</term><term>Binding Sites, Antibody</term><term>Chromatography, Affinity (methods)</term><term>Enzyme-Linked Immunosorbent Assay (methods)</term><term>Horseradish Peroxidase (chemistry)</term><term>Hybridomas (immunology)</term><term>Immunoenzyme Techniques</term><term>Rats</term><term>SARS Virus (immunology)</term><term>Sepharose (analogs & derivatives)</term><term>Sepharose (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Affinité des anticorps</term><term>Agarose ()</term><term>Agarose (analogues et dérivés)</term><term>Animaux</term><term>Anticorps antiviraux (isolement et purification)</term><term>Anticorps bispécifiques (isolement et purification)</term><term>Anticorps monoclonaux (immunologie)</term><term>Anticorps monoclonaux (isolement et purification)</term><term>Chromatographie d'affinité ()</term><term>Horseradish peroxidase ()</term><term>Hybridomes (immunologie)</term><term>Rats</term><term>Sites de fixation des anticorps</term><term>Techniques immunoenzymatiques</term><term>Test ELISA ()</term><term>Virus du SRAS (immunologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Sepharose</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Horseradish Peroxidase</term><term>Sepharose</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Antibodies, Monoclonal</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Antibodies, Bispecific</term><term>Antibodies, Monoclonal</term><term>Antibodies, Viral</term></keywords><keywords scheme="MESH" qualifier="analogues et dérivés" xml:lang="fr"><term>Agarose</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Anticorps monoclonaux</term><term>Hybridomes</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Hybridomas</term><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Anticorps antiviraux</term><term>Anticorps bispécifiques</term><term>Anticorps monoclonaux</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Chromatography, Affinity</term><term>Enzyme-Linked Immunosorbent Assay</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Antibody Affinity</term><term>Binding Sites, Antibody</term><term>Immunoenzyme Techniques</term><term>Rats</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Affinité des anticorps</term><term>Agarose</term><term>Animaux</term><term>Chromatographie d'affinité</term><term>Horseradish peroxidase</term><term>Rats</term><term>Sites de fixation des anticorps</term><term>Techniques immunoenzymatiques</term><term>Test ELISA</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Hybrid hybridomas (quadromas) are derived by fusing at least two hybridomas, each producing a different antibody of predefined specificity. The resulting cell secretes not only the immunoglobulins of both parents but also hybrid molecules manifesting the binding characteristics of the individual fusion partners. Purification of the desired bispecific immunoprobe with high specific activity from a mixture of bispecific and monospecific monoclonal antibodies requires special strategies. Using a dual, sequential affinity chromatography (Protein-G chromatography followed by m-aminophenyleboronic acid agarose column), we have purified bispecific monoclonal antibodies (BsMAb) as a preformed HRPO (Horseradish Peroxidase) complex (BsMAb-HRPO). The quadroma culture supernatant was initially processed on a Protein-G column to isolate all the species of immunoglobulins. This pre-enriched fraction was subsequently passed through the aminophenyleboronic acid column super saturated with HRPO. The column matrix has the ability to bind to proteins such as HRPO with vicinal diols. The enzyme loaded column captures the desired bispecific anti-SARS-CoVxanti-HRPO species with the elimination of the monospecific anti-SARS-CoV MAb to result in a high specific activity diagnostic probe. The presence of anti-HRPO MAb is an acceptable impurity as it will not bind to the target SARS-CoV NP antigen and will get washed out during the ELISA procedure.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18258500</PMID><DateCompleted><Year>2008</Year><Month>07</Month><Day>10</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">1570-0232</ISSN><JournalIssue CitedMedium="Print"><Volume>863</Volume><Issue>2</Issue><PubDate><Year>2008</Year><Month>Mar</Month><Day>01</Day></PubDate></JournalIssue><Title>Journal of chromatography. B, Analytical technologies in the biomedical and life sciences</Title><ISOAbbreviation>J. Chromatogr. B Analyt. Technol. Biomed. Life Sci.</ISOAbbreviation></Journal><ArticleTitle>Sequential affinity purification of peroxidase tagged bispecific anti-SARS-CoV antibodies on phenylboronic acid agarose.</ArticleTitle><Pagination><MedlinePgn>235-41</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.jchromb.2008.01.003</ELocationID><Abstract><AbstractText>Hybrid hybridomas (quadromas) are derived by fusing at least two hybridomas, each producing a different antibody of predefined specificity. The resulting cell secretes not only the immunoglobulins of both parents but also hybrid molecules manifesting the binding characteristics of the individual fusion partners. Purification of the desired bispecific immunoprobe with high specific activity from a mixture of bispecific and monospecific monoclonal antibodies requires special strategies. Using a dual, sequential affinity chromatography (Protein-G chromatography followed by m-aminophenyleboronic acid agarose column), we have purified bispecific monoclonal antibodies (BsMAb) as a preformed HRPO (Horseradish Peroxidase) complex (BsMAb-HRPO). The quadroma culture supernatant was initially processed on a Protein-G column to isolate all the species of immunoglobulins. This pre-enriched fraction was subsequently passed through the aminophenyleboronic acid column super saturated with HRPO. The column matrix has the ability to bind to proteins such as HRPO with vicinal diols. The enzyme loaded column captures the desired bispecific anti-SARS-CoVxanti-HRPO species with the elimination of the monospecific anti-SARS-CoV MAb to result in a high specific activity diagnostic probe. The presence of anti-HRPO MAb is an acceptable impurity as it will not bind to the target SARS-CoV NP antigen and will get washed out during the ELISA procedure.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Bhatnagar</LastName><ForeName>Pravin K</ForeName><Initials>PK</Initials><AffiliationInfo><Affiliation>Faculty of Pharmacy and Pharmaceutical Sciences, University of Alberta, Edmonton, Alberta, Canada T6G 2N8.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Das</LastName><ForeName>Dipankar</ForeName><Initials>D</Initials></Author><Author ValidYN="Y"><LastName>Suresh</LastName><ForeName>Mavanur R</ForeName><Initials>MR</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>U01 AI061233</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>U01 AI061233-04</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>5U01AI061233-02</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2008</Year><Month>01</Month><Day>17</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>J Chromatogr B Analyt Technol Biomed Life Sci</MedlineTA><NlmUniqueID>101139554</NlmUniqueID><ISSNLinking>1570-0232</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018033">Antibodies, Bispecific</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000911">Antibodies, 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Mavanur R" sort="Suresh, Mavanur R" uniqKey="Suresh M" first="Mavanur R" last="Suresh">Mavanur R. Suresh</name></noCountry><country name="Canada"><noRegion><name sortKey="Bhatnagar, Pravin K" sort="Bhatnagar, Pravin K" uniqKey="Bhatnagar P" first="Pravin K" last="Bhatnagar">Pravin K. Bhatnagar</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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