Monoclonal antibodies specific for apoproteins of lipophorins from the migratory locust
Spleen lymphocytes from mice immunized with locust native low‐density lipophorin A+ (LDLp) were fused with nonproducing myeloma cells, strain Sp 2/0. Hybridomas that were isolated from the fused cells produced antibodies specific for LDLp and the high‐density lipophorin Ayellow (HDLp). Monoclonal st...
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| Veröffentlicht in: | Archives of insect biochemistry and physiology 1987-10, Vol.6 (2), p.97-107 |
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| container_title | Archives of insect biochemistry and physiology |
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| creator | Schulz, T.K.F Van der Horst, D.J Amesz, H Voorma, H.O Beenakkers, A.M.T |
| description | Spleen lymphocytes from mice immunized with locust native low‐density lipophorin A+ (LDLp) were fused with nonproducing myeloma cells, strain Sp 2/0. Hybridomas that were isolated from the fused cells produced antibodies specific for LDLp and the high‐density lipophorin Ayellow (HDLp).
Monoclonal strains were generated through cloning by limiting dilution from those hybridomas synthesizing antibodies specific for apolipophorins (apoLp)‐I, ‐II, and ‐III of LDLp. Additionally, a hybridoma strain that was obtained after fusion of lymphocytes from mice immunized with apoLp‐III produced antibodies that bind to apoLp‐III and native LDLp.
Some features of LDLp and HDLp were studied using these antibodies. It could be demonstrated that apoLp‐I and apoLp‐II are not immunochemically identical and are exposed in the native particle of both LDLp and HDLp. It was also shown that in both lipophorins apoLp‐II is less exposed than apoLp‐I, whereas in LDLp apoLp‐III is mainly exposed; some apoLp‐III could also be detected in HDLp.
Tween‐20, a nonionic detergent, appears to affect the binding of anti‐apoLp‐I, ‐II, and ‐III to both LDLp and HDLp. The monoclonal antibodies specific for locust apolipophorins do not bind to the respective apoproteins of lipophorins from other insects. |
| doi_str_mv | 10.1002/arch.940060204 |
| format | Article |
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Monoclonal strains were generated through cloning by limiting dilution from those hybridomas synthesizing antibodies specific for apolipophorins (apoLp)‐I, ‐II, and ‐III of LDLp. Additionally, a hybridoma strain that was obtained after fusion of lymphocytes from mice immunized with apoLp‐III produced antibodies that bind to apoLp‐III and native LDLp.
Some features of LDLp and HDLp were studied using these antibodies. It could be demonstrated that apoLp‐I and apoLp‐II are not immunochemically identical and are exposed in the native particle of both LDLp and HDLp. It was also shown that in both lipophorins apoLp‐II is less exposed than apoLp‐I, whereas in LDLp apoLp‐III is mainly exposed; some apoLp‐III could also be detected in HDLp.
Tween‐20, a nonionic detergent, appears to affect the binding of anti‐apoLp‐I, ‐II, and ‐III to both LDLp and HDLp. The monoclonal antibodies specific for locust apolipophorins do not bind to the respective apoproteins of lipophorins from other insects.</description><identifier>ISSN: 0739-4462</identifier><identifier>EISSN: 1520-6327</identifier><identifier>DOI: 10.1002/arch.940060204</identifier><identifier>CODEN: AIBPEA</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>Acrididae ; ANTICORPS MONOCLONAL ; ANTICUERPOS MONOCLONALES ; apolipoproteins ; Biochemistry. Physiology. Immunology ; Biological and medical sciences ; CHEMISTRY ; CHIMIE ; ELISA ; Fundamental and applied biological sciences. Psychology ; hybridoma ; immunoblotting ; IMMUNOLOGICAL TECHNIQUES ; IMMUNOLOGIE ; IMMUNOLOGY ; INMUNOLOGIA ; Insecta ; Invertebrates ; LIPOPROTEINAS ; LIPOPROTEINE ; LIPOPROTEINS ; locust ; LOCUSTA ; LOCUSTA MIGRATORIA ; MONOCLONAL ANTIBODIES ; Orthoptera ; Physiology. Development ; QUIMICA ; TECHNIQUE IMMUNOLOGIQUE ; TECNICAS INMUNOLOGICAS</subject><ispartof>Archives of insect biochemistry and physiology, 1987-10, Vol.6 (2), p.97-107</ispartof><rights>Copyright © 1987 Wiley‐Liss, Inc.</rights><rights>1988 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4084-1919bc49bda8e3531a651aa251aa8d437fe379060a214f313973daf9acdfeae33</citedby><cites>FETCH-LOGICAL-c4084-1919bc49bda8e3531a651aa251aa8d437fe379060a214f313973daf9acdfeae33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Farch.940060204$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Farch.940060204$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27903,27904,45553,45554</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7436342$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Schulz, T.K.F</creatorcontrib><creatorcontrib>Van der Horst, D.J</creatorcontrib><creatorcontrib>Amesz, H</creatorcontrib><creatorcontrib>Voorma, H.O</creatorcontrib><creatorcontrib>Beenakkers, A.M.T</creatorcontrib><title>Monoclonal antibodies specific for apoproteins of lipophorins from the migratory locust</title><title>Archives of insect biochemistry and physiology</title><addtitle>Arch. Insect Biochem. Physiol</addtitle><description>Spleen lymphocytes from mice immunized with locust native low‐density lipophorin A+ (LDLp) were fused with nonproducing myeloma cells, strain Sp 2/0. Hybridomas that were isolated from the fused cells produced antibodies specific for LDLp and the high‐density lipophorin Ayellow (HDLp).
Monoclonal strains were generated through cloning by limiting dilution from those hybridomas synthesizing antibodies specific for apolipophorins (apoLp)‐I, ‐II, and ‐III of LDLp. Additionally, a hybridoma strain that was obtained after fusion of lymphocytes from mice immunized with apoLp‐III produced antibodies that bind to apoLp‐III and native LDLp.
Some features of LDLp and HDLp were studied using these antibodies. It could be demonstrated that apoLp‐I and apoLp‐II are not immunochemically identical and are exposed in the native particle of both LDLp and HDLp. It was also shown that in both lipophorins apoLp‐II is less exposed than apoLp‐I, whereas in LDLp apoLp‐III is mainly exposed; some apoLp‐III could also be detected in HDLp.
Tween‐20, a nonionic detergent, appears to affect the binding of anti‐apoLp‐I, ‐II, and ‐III to both LDLp and HDLp. The monoclonal antibodies specific for locust apolipophorins do not bind to the respective apoproteins of lipophorins from other insects.</description><subject>Acrididae</subject><subject>ANTICORPS MONOCLONAL</subject><subject>ANTICUERPOS MONOCLONALES</subject><subject>apolipoproteins</subject><subject>Biochemistry. Physiology. Immunology</subject><subject>Biological and medical sciences</subject><subject>CHEMISTRY</subject><subject>CHIMIE</subject><subject>ELISA</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>hybridoma</subject><subject>immunoblotting</subject><subject>IMMUNOLOGICAL TECHNIQUES</subject><subject>IMMUNOLOGIE</subject><subject>IMMUNOLOGY</subject><subject>INMUNOLOGIA</subject><subject>Insecta</subject><subject>Invertebrates</subject><subject>LIPOPROTEINAS</subject><subject>LIPOPROTEINE</subject><subject>LIPOPROTEINS</subject><subject>locust</subject><subject>LOCUSTA</subject><subject>LOCUSTA MIGRATORIA</subject><subject>MONOCLONAL ANTIBODIES</subject><subject>Orthoptera</subject><subject>Physiology. Development</subject><subject>QUIMICA</subject><subject>TECHNIQUE IMMUNOLOGIQUE</subject><subject>TECNICAS INMUNOLOGICAS</subject><issn>0739-4462</issn><issn>1520-6327</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><recordid>eNqFkEFrGzEQhUVpoW6aa0896FB6W0fSaFerYzBtHEhSSBqSmxhrpVitvHKlNY3_fdZsML31MsPA997MPEI-cTbnjIkzzHY915Kxhgkm35AZrwWrGhDqLZkxBbqSshHvyYdSfjHGdMPbGXm4Tn2yMfUYKfZDWKUuuELL1tngg6U-ZYrbtM1pcKEvNHkawzivUz6MPqcNHdaObsJTxiHlPY3J7srwkbzzGIs7fe0n5P77t5-LZXX14-JycX5VWclaWXHN9cpKveqwdVADx6bmiOJQ2k6C8g6UHj9CwaUHDlpBh16j7bxDB3BCvk6-44V_dq4MZhOKdTFi79KuGF4DKC7ZCM4n0OZUSnbebHPYYN4bzswhP3PIzxzzGwVfXp2xWIw-Y29DOaqUhAakGDE9YX9DdPv_mJrz28Xy3xXVpA1lcM9HLebfplGgavNwc2Fu7wQ8Lq9rczPynyfeYzL4lMdz7u_alssGWNvCC_SZmpg</recordid><startdate>198710</startdate><enddate>198710</enddate><creator>Schulz, T.K.F</creator><creator>Van der Horst, D.J</creator><creator>Amesz, H</creator><creator>Voorma, H.O</creator><creator>Beenakkers, A.M.T</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><general>Wiley-Liss</general><scope>FBQ</scope><scope>BSCLL</scope><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7SS</scope></search><sort><creationdate>198710</creationdate><title>Monoclonal antibodies specific for apoproteins of lipophorins from the migratory locust</title><author>Schulz, T.K.F ; Van der Horst, D.J ; Amesz, H ; Voorma, H.O ; Beenakkers, A.M.T</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4084-1919bc49bda8e3531a651aa251aa8d437fe379060a214f313973daf9acdfeae33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Acrididae</topic><topic>ANTICORPS MONOCLONAL</topic><topic>ANTICUERPOS MONOCLONALES</topic><topic>apolipoproteins</topic><topic>Biochemistry. Physiology. Immunology</topic><topic>Biological and medical sciences</topic><topic>CHEMISTRY</topic><topic>CHIMIE</topic><topic>ELISA</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>hybridoma</topic><topic>immunoblotting</topic><topic>IMMUNOLOGICAL TECHNIQUES</topic><topic>IMMUNOLOGIE</topic><topic>IMMUNOLOGY</topic><topic>INMUNOLOGIA</topic><topic>Insecta</topic><topic>Invertebrates</topic><topic>LIPOPROTEINAS</topic><topic>LIPOPROTEINE</topic><topic>LIPOPROTEINS</topic><topic>locust</topic><topic>LOCUSTA</topic><topic>LOCUSTA MIGRATORIA</topic><topic>MONOCLONAL ANTIBODIES</topic><topic>Orthoptera</topic><topic>Physiology. Development</topic><topic>QUIMICA</topic><topic>TECHNIQUE IMMUNOLOGIQUE</topic><topic>TECNICAS INMUNOLOGICAS</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Schulz, T.K.F</creatorcontrib><creatorcontrib>Van der Horst, D.J</creatorcontrib><creatorcontrib>Amesz, H</creatorcontrib><creatorcontrib>Voorma, H.O</creatorcontrib><creatorcontrib>Beenakkers, A.M.T</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Entomology Abstracts (Full archive)</collection><jtitle>Archives of insect biochemistry and physiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Schulz, T.K.F</au><au>Van der Horst, D.J</au><au>Amesz, H</au><au>Voorma, H.O</au><au>Beenakkers, A.M.T</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Monoclonal antibodies specific for apoproteins of lipophorins from the migratory locust</atitle><jtitle>Archives of insect biochemistry and physiology</jtitle><addtitle>Arch. Insect Biochem. Physiol</addtitle><date>1987-10</date><risdate>1987</risdate><volume>6</volume><issue>2</issue><spage>97</spage><epage>107</epage><pages>97-107</pages><issn>0739-4462</issn><eissn>1520-6327</eissn><coden>AIBPEA</coden><abstract>Spleen lymphocytes from mice immunized with locust native low‐density lipophorin A+ (LDLp) were fused with nonproducing myeloma cells, strain Sp 2/0. Hybridomas that were isolated from the fused cells produced antibodies specific for LDLp and the high‐density lipophorin Ayellow (HDLp).
Monoclonal strains were generated through cloning by limiting dilution from those hybridomas synthesizing antibodies specific for apolipophorins (apoLp)‐I, ‐II, and ‐III of LDLp. Additionally, a hybridoma strain that was obtained after fusion of lymphocytes from mice immunized with apoLp‐III produced antibodies that bind to apoLp‐III and native LDLp.
Some features of LDLp and HDLp were studied using these antibodies. It could be demonstrated that apoLp‐I and apoLp‐II are not immunochemically identical and are exposed in the native particle of both LDLp and HDLp. It was also shown that in both lipophorins apoLp‐II is less exposed than apoLp‐I, whereas in LDLp apoLp‐III is mainly exposed; some apoLp‐III could also be detected in HDLp.
Tween‐20, a nonionic detergent, appears to affect the binding of anti‐apoLp‐I, ‐II, and ‐III to both LDLp and HDLp. The monoclonal antibodies specific for locust apolipophorins do not bind to the respective apoproteins of lipophorins from other insects.</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><doi>10.1002/arch.940060204</doi><tpages>11</tpages></addata></record> |
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| identifier | ISSN: 0739-4462 |
| ispartof | Archives of insect biochemistry and physiology, 1987-10, Vol.6 (2), p.97-107 |
| issn | 0739-4462 1520-6327 |
| language | eng |
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| source | Wiley Online Library Journals Frontfile Complete |
| subjects | Acrididae ANTICORPS MONOCLONAL ANTICUERPOS MONOCLONALES apolipoproteins Biochemistry. Physiology. Immunology Biological and medical sciences CHEMISTRY CHIMIE ELISA Fundamental and applied biological sciences. Psychology hybridoma immunoblotting IMMUNOLOGICAL TECHNIQUES IMMUNOLOGIE IMMUNOLOGY INMUNOLOGIA Insecta Invertebrates LIPOPROTEINAS LIPOPROTEINE LIPOPROTEINS locust LOCUSTA LOCUSTA MIGRATORIA MONOCLONAL ANTIBODIES Orthoptera Physiology. Development QUIMICA TECHNIQUE IMMUNOLOGIQUE TECNICAS INMUNOLOGICAS |
| title | Monoclonal antibodies specific for apoproteins of lipophorins from the migratory locust |
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