Characterization of Mouse Monoclonal Antibodies to Human Interferon-Gamma
Mouse monoclonal antibodies (mAb) to human interferon-gamma (HuIFN-γ) were characterized. The mAbs studied-E4-18, G4-15, and SAT-1-which are all IgG1-type, reacted to all HuIFN-γ molecular species, both glycosylated and non-glycosylated. Affinity constants calculated of E4-18 and G4-15 didn't h...
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Veröffentlicht in: | MICROBIOLOGY and IMMUNOLOGY 1988, Vol.32(4), pp.339-350 |
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description | Mouse monoclonal antibodies (mAb) to human interferon-gamma (HuIFN-γ) were characterized. The mAbs studied-E4-18, G4-15, and SAT-1-which are all IgG1-type, reacted to all HuIFN-γ molecular species, both glycosylated and non-glycosylated. Affinity constants calculated of E4-18 and G4-15 didn't have considerable differences for both kinds of HuIFN-γ (1-3×108liter/mol), but SAT-1 had a difference-a higher value (1010liter/mol) for the former than for the latter (8×108liter/mol). In epitope specificity, the results suggested that E4-18 and G4-15 recognized an overlapped region remote from the region of SAT-1. Competition experiment using synthetic peptides suggested that epitope of G4-15 is around N9-26 of the HuIFN-γ sequence. Those mAbs could be used for sandwich radioimmunoassay of HuIFN-γ using double mAbs in two combinations, one (G4-15/E4-18) based on dimer forms of HuIFN-γ and the other (SAT-1/E4-18) based on epitope difference. The mAbs are all neutralizing antibodies in which SAT-1 neutralized at a lower concentration than did G4-15, and at a much lower one than did E4-18. The receptor binding of HuIFN-γ was inhibited by mAbs G4-15 and SAT-1. Efficacy of G4-15 and SAT-1 for the inhibition correspond with that for neutralization. |
doi_str_mv | 10.1111/j.1348-0421.1988.tb01394.x |
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The mAbs studied-E4-18, G4-15, and SAT-1-which are all IgG1-type, reacted to all HuIFN-γ molecular species, both glycosylated and non-glycosylated. Affinity constants calculated of E4-18 and G4-15 didn't have considerable differences for both kinds of HuIFN-γ (1-3×108liter/mol), but SAT-1 had a difference-a higher value (1010liter/mol) for the former than for the latter (8×108liter/mol). In epitope specificity, the results suggested that E4-18 and G4-15 recognized an overlapped region remote from the region of SAT-1. Competition experiment using synthetic peptides suggested that epitope of G4-15 is around N9-26 of the HuIFN-γ sequence. Those mAbs could be used for sandwich radioimmunoassay of HuIFN-γ using double mAbs in two combinations, one (G4-15/E4-18) based on dimer forms of HuIFN-γ and the other (SAT-1/E4-18) based on epitope difference. The mAbs are all neutralizing antibodies in which SAT-1 neutralized at a lower concentration than did G4-15, and at a much lower one than did E4-18. The receptor binding of HuIFN-γ was inhibited by mAbs G4-15 and SAT-1. Efficacy of G4-15 and SAT-1 for the inhibition correspond with that for neutralization.</description><identifier>ISSN: 0385-5600</identifier><identifier>EISSN: 1348-0421</identifier><identifier>DOI: 10.1111/j.1348-0421.1988.tb01394.x</identifier><identifier>PMID: 2455856</identifier><identifier>CODEN: MIIMDV</identifier><language>eng</language><publisher>Tokyo: Blackwell Publishing Ltd</publisher><subject>Analysis of the immune response. Humoral and cellular immunity ; Animals ; Antibodies, Monoclonal - analysis ; Antibodies, Monoclonal - immunology ; Antibodies, Monoclonal - metabolism ; Biological and medical sciences ; Epitopes - immunology ; Fundamental and applied biological sciences. Psychology ; Fundamental immunology ; Humans ; Immunobiology ; Interferon-gamma - analysis ; Interferon-gamma - immunology ; Interferon-gamma - metabolism ; Mice ; Mice, Inbred BALB C ; Miscellaneous ; Neutralization Tests ; Radioimmunoassay ; Receptors, Immunologic - metabolism ; Receptors, Interferon ; Regulatory factors and their cellular receptors</subject><ispartof>MICROBIOLOGY and IMMUNOLOGY, 1988, Vol.32(4), pp.339-350</ispartof><rights>Center for Academic Publications Japan</rights><rights>owned by Center for Academic Publications Japan (Publisher)</rights><rights>1989 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c7314-5c2d144b62d077e5bf73af7894d145946fed0d747b2923095e9f4215de7696d93</citedby><cites>FETCH-LOGICAL-c7314-5c2d144b62d077e5bf73af7894d145946fed0d747b2923095e9f4215de7696d93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,1876,27903,27904</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7232592$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2455856$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yamamoto, Yoko</creatorcontrib><creatorcontrib>Miyata, Keizo</creatorcontrib><creatorcontrib>Ueda, Masamichi</creatorcontrib><creatorcontrib>Kawade, Yoshimi</creatorcontrib><creatorcontrib>Matsumoto, Kayoko</creatorcontrib><creatorcontrib>Tsukui, Kazuo</creatorcontrib><title>Characterization of Mouse Monoclonal Antibodies to Human Interferon-Gamma</title><title>MICROBIOLOGY and IMMUNOLOGY</title><addtitle>Microbiology and Immunology</addtitle><description>Mouse monoclonal antibodies (mAb) to human interferon-gamma (HuIFN-γ) were characterized. The mAbs studied-E4-18, G4-15, and SAT-1-which are all IgG1-type, reacted to all HuIFN-γ molecular species, both glycosylated and non-glycosylated. Affinity constants calculated of E4-18 and G4-15 didn't have considerable differences for both kinds of HuIFN-γ (1-3×108liter/mol), but SAT-1 had a difference-a higher value (1010liter/mol) for the former than for the latter (8×108liter/mol). In epitope specificity, the results suggested that E4-18 and G4-15 recognized an overlapped region remote from the region of SAT-1. Competition experiment using synthetic peptides suggested that epitope of G4-15 is around N9-26 of the HuIFN-γ sequence. Those mAbs could be used for sandwich radioimmunoassay of HuIFN-γ using double mAbs in two combinations, one (G4-15/E4-18) based on dimer forms of HuIFN-γ and the other (SAT-1/E4-18) based on epitope difference. The mAbs are all neutralizing antibodies in which SAT-1 neutralized at a lower concentration than did G4-15, and at a much lower one than did E4-18. The receptor binding of HuIFN-γ was inhibited by mAbs G4-15 and SAT-1. Efficacy of G4-15 and SAT-1 for the inhibition correspond with that for neutralization.</description><subject>Analysis of the immune response. Humoral and cellular immunity</subject><subject>Animals</subject><subject>Antibodies, Monoclonal - analysis</subject><subject>Antibodies, Monoclonal - immunology</subject><subject>Antibodies, Monoclonal - metabolism</subject><subject>Biological and medical sciences</subject><subject>Epitopes - immunology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fundamental immunology</subject><subject>Humans</subject><subject>Immunobiology</subject><subject>Interferon-gamma - analysis</subject><subject>Interferon-gamma - immunology</subject><subject>Interferon-gamma - metabolism</subject><subject>Mice</subject><subject>Mice, Inbred BALB C</subject><subject>Miscellaneous</subject><subject>Neutralization Tests</subject><subject>Radioimmunoassay</subject><subject>Receptors, Immunologic - metabolism</subject><subject>Receptors, Interferon</subject><subject>Regulatory factors and their cellular receptors</subject><issn>0385-5600</issn><issn>1348-0421</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1988</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkl1v0zAUhi0EGl3hJyBFCCFuEvztmKuNanRFK0gI1EvLcRxwSZxhp1rHr8clUcQVCF8cWz7veXzs1wA8R7BAabzeF4jQMocUowLJsiyGCiIiaXF8ABZz6iFYQFKynHEIH4PzGPcQYoFLegbOMGWsZHwBNqtvOmgz2OB-6sH1PuubbNsfok3R96btvW6zSz-4qq-djdnQZ9eHTvts41NRY0Pv87XuOv0EPGp0G-3TaV6CL--uPq-u85uP683q8iY3giCaM4NrRGnFcQ2FsKxqBNGNKCVN20xS3tga1oKKCktMoGRWNukyrLaCS15LsgQvR-5t6H8cbBxU56Kxbau9TX0rURKEuOBJ-OqvQkQl5oQQTP7JTFKUeoFJ-GYUmtDHGGyjboPrdLhXCKqTN2qvTgaokwHq5I2avFHHVPxsOuVQdbaeSyczUv7FlNfR6LYJ2hsXZ5nABLP0JktwMcruXGvv_6MBtd1sfy8T4mpE7OOgv9qZocPgTGtV8rd2SAqhCFZ0CkTOeZM-jbI-cfKR4-Jgj39gvisuiGBq92Gt3qIdp5-2O_We_AI_vNGr</recordid><startdate>19880101</startdate><enddate>19880101</enddate><creator>Yamamoto, Yoko</creator><creator>Miyata, Keizo</creator><creator>Ueda, Masamichi</creator><creator>Kawade, Yoshimi</creator><creator>Matsumoto, Kayoko</creator><creator>Tsukui, Kazuo</creator><general>Blackwell Publishing Ltd</general><general>Center For Academic Publications Japan</general><general>Center for Academic Publications Japan</general><scope>BSCLL</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7T5</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>19880101</creationdate><title>Characterization of Mouse Monoclonal Antibodies to Human Interferon-Gamma</title><author>Yamamoto, Yoko ; Miyata, Keizo ; Ueda, Masamichi ; Kawade, Yoshimi ; Matsumoto, Kayoko ; Tsukui, Kazuo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c7314-5c2d144b62d077e5bf73af7894d145946fed0d747b2923095e9f4215de7696d93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1988</creationdate><topic>Analysis of the immune response. Humoral and cellular immunity</topic><topic>Animals</topic><topic>Antibodies, Monoclonal - analysis</topic><topic>Antibodies, Monoclonal - immunology</topic><topic>Antibodies, Monoclonal - metabolism</topic><topic>Biological and medical sciences</topic><topic>Epitopes - immunology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fundamental immunology</topic><topic>Humans</topic><topic>Immunobiology</topic><topic>Interferon-gamma - analysis</topic><topic>Interferon-gamma - immunology</topic><topic>Interferon-gamma - metabolism</topic><topic>Mice</topic><topic>Mice, Inbred BALB C</topic><topic>Miscellaneous</topic><topic>Neutralization Tests</topic><topic>Radioimmunoassay</topic><topic>Receptors, Immunologic - metabolism</topic><topic>Receptors, Interferon</topic><topic>Regulatory factors and their cellular receptors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yamamoto, Yoko</creatorcontrib><creatorcontrib>Miyata, Keizo</creatorcontrib><creatorcontrib>Ueda, Masamichi</creatorcontrib><creatorcontrib>Kawade, Yoshimi</creatorcontrib><creatorcontrib>Matsumoto, Kayoko</creatorcontrib><creatorcontrib>Tsukui, Kazuo</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Immunology Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>MICROBIOLOGY and IMMUNOLOGY</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yamamoto, Yoko</au><au>Miyata, Keizo</au><au>Ueda, Masamichi</au><au>Kawade, Yoshimi</au><au>Matsumoto, Kayoko</au><au>Tsukui, Kazuo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of Mouse Monoclonal Antibodies to Human Interferon-Gamma</atitle><jtitle>MICROBIOLOGY and IMMUNOLOGY</jtitle><addtitle>Microbiology and Immunology</addtitle><date>1988-01-01</date><risdate>1988</risdate><volume>32</volume><issue>4</issue><spage>339</spage><epage>350</epage><pages>339-350</pages><issn>0385-5600</issn><eissn>1348-0421</eissn><coden>MIIMDV</coden><abstract>Mouse monoclonal antibodies (mAb) to human interferon-gamma (HuIFN-γ) were characterized. The mAbs studied-E4-18, G4-15, and SAT-1-which are all IgG1-type, reacted to all HuIFN-γ molecular species, both glycosylated and non-glycosylated. Affinity constants calculated of E4-18 and G4-15 didn't have considerable differences for both kinds of HuIFN-γ (1-3×108liter/mol), but SAT-1 had a difference-a higher value (1010liter/mol) for the former than for the latter (8×108liter/mol). In epitope specificity, the results suggested that E4-18 and G4-15 recognized an overlapped region remote from the region of SAT-1. Competition experiment using synthetic peptides suggested that epitope of G4-15 is around N9-26 of the HuIFN-γ sequence. Those mAbs could be used for sandwich radioimmunoassay of HuIFN-γ using double mAbs in two combinations, one (G4-15/E4-18) based on dimer forms of HuIFN-γ and the other (SAT-1/E4-18) based on epitope difference. The mAbs are all neutralizing antibodies in which SAT-1 neutralized at a lower concentration than did G4-15, and at a much lower one than did E4-18. The receptor binding of HuIFN-γ was inhibited by mAbs G4-15 and SAT-1. Efficacy of G4-15 and SAT-1 for the inhibition correspond with that for neutralization.</abstract><cop>Tokyo</cop><pub>Blackwell Publishing Ltd</pub><pmid>2455856</pmid><doi>10.1111/j.1348-0421.1988.tb01394.x</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Analysis of the immune response. Humoral and cellular immunity Animals Antibodies, Monoclonal - analysis Antibodies, Monoclonal - immunology Antibodies, Monoclonal - metabolism Biological and medical sciences Epitopes - immunology Fundamental and applied biological sciences. Psychology Fundamental immunology Humans Immunobiology Interferon-gamma - analysis Interferon-gamma - immunology Interferon-gamma - metabolism Mice Mice, Inbred BALB C Miscellaneous Neutralization Tests Radioimmunoassay Receptors, Immunologic - metabolism Receptors, Interferon Regulatory factors and their cellular receptors |
title | Characterization of Mouse Monoclonal Antibodies to Human Interferon-Gamma |
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