Binding studies on anti-fructofuranan mouse myeloma immunoglobulins A47N, A4, U61, and E109
Four murine myeloma immunoglobulins, A4, A47N, U61, and E109, have been studied for their binding affinities with inulin and a series of oligosaccharides derived from inulin. The results indicate that the combining site of these immunoglobulins shows highest complementarity for a trifructofuranosyl...
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| Veröffentlicht in: | Biochemistry (Easton) 1977-08, Vol.16 (17), p.3760-3765 |
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| container_issue | 17 |
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| container_title | Biochemistry (Easton) |
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| creator | Streefkerk, D. G Glaudemans, C. P. J |
| description | Four murine myeloma immunoglobulins, A4, A47N, U61, and E109, have been studied for their binding affinities with inulin and a series of oligosaccharides derived from inulin. The results indicate that the combining site of these immunoglobulins shows highest complementarity for a trifructofuranosyl sequence (A4 and A47N) and a tetrafructofuranosyl sequence (U61 and E109). The size of the combining area of the immunoglobulin E109 derived from the antigenic determinant (approximately 15 X 14 X 10 A) agrees well with the size observed on a hypothetical space model of the Fv portion of E109 (Potter, M., Rudikoff, S., Padlan, E. A., and Vrana, M. (1976), Antibodies in Human Diagnosis and Therapy, Haber, E., and Krause, R.M., Ed., New York, N.Y., Raven Press). |
| doi_str_mv | 10.1021/bi00636a005 |
| format | Article |
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(1976), Antibodies in Human Diagnosis and Therapy, Haber, E., and Krause, R.M., Ed., New York, N.Y., Raven Press).</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi00636a005</identifier><identifier>PMID: 901750</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Animals ; Binding Sites, Antibody ; Carbohydrates - immunology ; Fructose - immunology ; Immunoglobulin A ; Immunoglobulin Fab Fragments ; Inulin - immunology ; Ligands ; Mice ; Models, Molecular ; Molecular Conformation ; Myeloma Proteins ; Plasmacytoma - immunology ; Precipitin Tests ; Spectrometry, Fluorescence</subject><ispartof>Biochemistry (Easton), 1977-08, Vol.16 (17), p.3760-3765</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a353t-221bfef6b85665f8eb81b86407af2fabed22945d5aec76bc98863fbf1305b2083</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bi00636a005$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi00636a005$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,2765,27076,27924,27925,56738,56788</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/901750$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Streefkerk, D. G</creatorcontrib><creatorcontrib>Glaudemans, C. P. J</creatorcontrib><title>Binding studies on anti-fructofuranan mouse myeloma immunoglobulins A47N, A4, U61, and E109</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>Four murine myeloma immunoglobulins, A4, A47N, U61, and E109, have been studied for their binding affinities with inulin and a series of oligosaccharides derived from inulin. The results indicate that the combining site of these immunoglobulins shows highest complementarity for a trifructofuranosyl sequence (A4 and A47N) and a tetrafructofuranosyl sequence (U61 and E109). The size of the combining area of the immunoglobulin E109 derived from the antigenic determinant (approximately 15 X 14 X 10 A) agrees well with the size observed on a hypothetical space model of the Fv portion of E109 (Potter, M., Rudikoff, S., Padlan, E. A., and Vrana, M. (1976), Antibodies in Human Diagnosis and Therapy, Haber, E., and Krause, R.M., Ed., New York, N.Y., Raven Press).</description><subject>Animals</subject><subject>Binding Sites, Antibody</subject><subject>Carbohydrates - immunology</subject><subject>Fructose - immunology</subject><subject>Immunoglobulin A</subject><subject>Immunoglobulin Fab Fragments</subject><subject>Inulin - immunology</subject><subject>Ligands</subject><subject>Mice</subject><subject>Models, Molecular</subject><subject>Molecular Conformation</subject><subject>Myeloma Proteins</subject><subject>Plasmacytoma - immunology</subject><subject>Precipitin Tests</subject><subject>Spectrometry, Fluorescence</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1977</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkL1P3jAQxi3U0r4FJtYOnujQN-XsxE48AqIfAgoSsMBg2YmNTBMb7Fgq_z1GQahDlzudnt_dPXoQ2iXwjQAl-9oB8JorALaBVoRRqBoh2Du0giJUVHD4iD6ldF_GBtrmA9oUQFoGK3R76Pzg_B1Ocx6cSTh4rPzsKhtzPwebo_LK4ynkZPD0ZMYwKeymKftwNwadR-cTPmja3-tS1_iak3XZH_AxAbGN3ls1JrPz2rfQ9ffjq6Of1en5j19HB6eVqlk9V5QSbY3lumOcM9sZ3RHd8WJUWWqVNgOlomEDU6Zvue5F1_HaaktqYJpCV2-hveXuQwyP2aRZTi71ZhyVN8W37BoQhLWigF8XsI8hpWisfIhuUvFJEpAvScp_kiz059ezWU9meGOX6IpcLbJLs_n7pqr4R_K2bpm8uriUZ01NT27gQtLCf1l41Sd5H3L0JZP_Pn4Gz8eHjw</recordid><startdate>19770823</startdate><enddate>19770823</enddate><creator>Streefkerk, D. G</creator><creator>Glaudemans, C. P. J</creator><general>American Chemical Society</general><scope>BSCLL</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>7X8</scope></search><sort><creationdate>19770823</creationdate><title>Binding studies on anti-fructofuranan mouse myeloma immunoglobulins A47N, A4, U61, and E109</title><author>Streefkerk, D. G ; Glaudemans, C. P. J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a353t-221bfef6b85665f8eb81b86407af2fabed22945d5aec76bc98863fbf1305b2083</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1977</creationdate><topic>Animals</topic><topic>Binding Sites, Antibody</topic><topic>Carbohydrates - immunology</topic><topic>Fructose - immunology</topic><topic>Immunoglobulin A</topic><topic>Immunoglobulin Fab Fragments</topic><topic>Inulin - immunology</topic><topic>Ligands</topic><topic>Mice</topic><topic>Models, Molecular</topic><topic>Molecular Conformation</topic><topic>Myeloma Proteins</topic><topic>Plasmacytoma - immunology</topic><topic>Precipitin Tests</topic><topic>Spectrometry, Fluorescence</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Streefkerk, D. G</creatorcontrib><creatorcontrib>Glaudemans, C. P. J</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Streefkerk, D. G</au><au>Glaudemans, C. P. J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Binding studies on anti-fructofuranan mouse myeloma immunoglobulins A47N, A4, U61, and E109</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>1977-08-23</date><risdate>1977</risdate><volume>16</volume><issue>17</issue><spage>3760</spage><epage>3765</epage><pages>3760-3765</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>Four murine myeloma immunoglobulins, A4, A47N, U61, and E109, have been studied for their binding affinities with inulin and a series of oligosaccharides derived from inulin. The results indicate that the combining site of these immunoglobulins shows highest complementarity for a trifructofuranosyl sequence (A4 and A47N) and a tetrafructofuranosyl sequence (U61 and E109). The size of the combining area of the immunoglobulin E109 derived from the antigenic determinant (approximately 15 X 14 X 10 A) agrees well with the size observed on a hypothetical space model of the Fv portion of E109 (Potter, M., Rudikoff, S., Padlan, E. A., and Vrana, M. (1976), Antibodies in Human Diagnosis and Therapy, Haber, E., and Krause, R.M., Ed., New York, N.Y., Raven Press).</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>901750</pmid><doi>10.1021/bi00636a005</doi><tpages>6</tpages></addata></record> |
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| ispartof | Biochemistry (Easton), 1977-08, Vol.16 (17), p.3760-3765 |
| issn | 0006-2960 1520-4995 |
| language | eng |
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| source | MEDLINE; ACS Publications |
| subjects | Animals Binding Sites, Antibody Carbohydrates - immunology Fructose - immunology Immunoglobulin A Immunoglobulin Fab Fragments Inulin - immunology Ligands Mice Models, Molecular Molecular Conformation Myeloma Proteins Plasmacytoma - immunology Precipitin Tests Spectrometry, Fluorescence |
| title | Binding studies on anti-fructofuranan mouse myeloma immunoglobulins A47N, A4, U61, and E109 |
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