Structural composition of canine secretory component and immunoglobulin A
Dog serum and colostral immunoglobulin A (IgA) and free secretory component from colostrum were isolated using affinity chromatography. Both serum and colostral IgA showed similar susceptibility to reduction with dithiothreitol, but only colostral IgA released the additional subunit, bound secretory...
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Veröffentlicht in: | Biochemistry (Easton) 1975-07, Vol.14 (13), p.2853-2860 |
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creator | Thompson, Russell E Reynolds, Herbert Y Waxdal, Myron J |
description | Dog serum and colostral immunoglobulin A (IgA) and free secretory component from colostrum were isolated using affinity chromatography. Both serum and colostral IgA showed similar susceptibility to reduction with dithiothreitol, but only colostral IgA released the additional subunit, bound secretory component. This released secretory component was identical with free secretory component with respect to electrophoretic migration, isoelectric focusing point, and molecular weight, but lacked some antigenic determinants. The amino acid composition and the N-terminal sequence of canine free secretory component was similar to that reported for the cow. |
doi_str_mv | 10.1021/bi00684a010 |
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Both serum and colostral IgA showed similar susceptibility to reduction with dithiothreitol, but only colostral IgA released the additional subunit, bound secretory component. This released secretory component was identical with free secretory component with respect to electrophoretic migration, isoelectric focusing point, and molecular weight, but lacked some antigenic determinants. The amino acid composition and the N-terminal sequence of canine free secretory component was similar to that reported for the cow.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi00684a010</identifier><identifier>PMID: 807240</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Amino Acids - analysis ; Animals ; Chromatography, Affinity ; Chromatography, Gel ; Colostrum - immunology ; Cross Reactions ; Dithiothreitol - pharmacology ; Dogs ; Electrophoresis, Polyacrylamide Gel ; Female ; Immunodiffusion ; Immunoelectrophoresis ; Immunoglobulin A - analysis ; Immunoglobulin A - isolation & purification ; Immunoglobulin A - metabolism ; Immunoglobulin Fragments - analysis ; Immunoglobulin Fragments - isolation & purification ; Immunoglobulin Fragments - metabolism ; Isoelectric Focusing ; Methods ; Molecular Weight ; Peptide Fragments - analysis ; Protein Binding ; Rabbits - immunology</subject><ispartof>Biochemistry (Easton), 1975-07, Vol.14 (13), p.2853-2860</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a353t-df767d911966428af5c2d92a523d874391aa70839ea939858d11a7a3389a12f3</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/bi00684a010$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi00684a010$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,776,780,2752,27055,27903,27904,56716,56766</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/807240$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Thompson, Russell E</creatorcontrib><creatorcontrib>Reynolds, Herbert Y</creatorcontrib><creatorcontrib>Waxdal, Myron J</creatorcontrib><title>Structural composition of canine secretory component and immunoglobulin A</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>Dog serum and colostral immunoglobulin A (IgA) and free secretory component from colostrum were isolated using affinity chromatography. Both serum and colostral IgA showed similar susceptibility to reduction with dithiothreitol, but only colostral IgA released the additional subunit, bound secretory component. This released secretory component was identical with free secretory component with respect to electrophoretic migration, isoelectric focusing point, and molecular weight, but lacked some antigenic determinants. The amino acid composition and the N-terminal sequence of canine free secretory component was similar to that reported for the cow.</description><subject>Amino Acids - analysis</subject><subject>Animals</subject><subject>Chromatography, Affinity</subject><subject>Chromatography, Gel</subject><subject>Colostrum - immunology</subject><subject>Cross Reactions</subject><subject>Dithiothreitol - pharmacology</subject><subject>Dogs</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Female</subject><subject>Immunodiffusion</subject><subject>Immunoelectrophoresis</subject><subject>Immunoglobulin A - analysis</subject><subject>Immunoglobulin A - isolation & purification</subject><subject>Immunoglobulin A - metabolism</subject><subject>Immunoglobulin Fragments - analysis</subject><subject>Immunoglobulin Fragments - isolation & purification</subject><subject>Immunoglobulin Fragments - metabolism</subject><subject>Isoelectric Focusing</subject><subject>Methods</subject><subject>Molecular Weight</subject><subject>Peptide Fragments - analysis</subject><subject>Protein Binding</subject><subject>Rabbits - immunology</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1975</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkEtLw0AQgBfxVasnrx5y0oNE95Xs7rHURwsFC-19mSYb2Zrs1t0E7L83EikePA3D9zEDH0LXBD8QTMnjxmKcSw6Y4CM0IhnFKVcqO0Yj3IOUqhyfo4sYt_3KseBn6FRiQTkeofmqDV3RdgHqpPDNzkfbWu8SXyUFOOtMEk0RTOvDfuDOuDYBVya2aTrn32u_6WrrksklOqmgjubqd47R-uV5PZ2li7fX-XSySIFlrE3LSuSiVISoPOdUQpUVtFQUMspKKThTBEBgyZQBxZTMZEkICGBMKiC0YmN0O5zdBf_ZmdjqxsbC1DU447uoJVWYcp734v0gFsHHGEyld8E2EPaaYP2TTf_J1ts3v2e7TWPKgzt06nE6YBtb83WgED50LpjI9Hq50uppRtRitdS89-8GH4qot74Lrk_y7-NvA2KClQ</recordid><startdate>19750701</startdate><enddate>19750701</enddate><creator>Thompson, Russell E</creator><creator>Reynolds, Herbert Y</creator><creator>Waxdal, Myron 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>19750701</creationdate><title>Structural composition of canine secretory component and immunoglobulin A</title><author>Thompson, Russell E ; Reynolds, Herbert Y ; Waxdal, Myron J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a353t-df767d911966428af5c2d92a523d874391aa70839ea939858d11a7a3389a12f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1975</creationdate><topic>Amino Acids - analysis</topic><topic>Animals</topic><topic>Chromatography, Affinity</topic><topic>Chromatography, Gel</topic><topic>Colostrum - immunology</topic><topic>Cross Reactions</topic><topic>Dithiothreitol - pharmacology</topic><topic>Dogs</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Female</topic><topic>Immunodiffusion</topic><topic>Immunoelectrophoresis</topic><topic>Immunoglobulin A - analysis</topic><topic>Immunoglobulin A - isolation & purification</topic><topic>Immunoglobulin A - metabolism</topic><topic>Immunoglobulin Fragments - analysis</topic><topic>Immunoglobulin Fragments - isolation & purification</topic><topic>Immunoglobulin Fragments - metabolism</topic><topic>Isoelectric Focusing</topic><topic>Methods</topic><topic>Molecular Weight</topic><topic>Peptide Fragments - analysis</topic><topic>Protein Binding</topic><topic>Rabbits - immunology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Thompson, Russell E</creatorcontrib><creatorcontrib>Reynolds, Herbert Y</creatorcontrib><creatorcontrib>Waxdal, Myron 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>Thompson, Russell E</au><au>Reynolds, Herbert Y</au><au>Waxdal, Myron J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural composition of canine secretory component and immunoglobulin A</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>1975-07-01</date><risdate>1975</risdate><volume>14</volume><issue>13</issue><spage>2853</spage><epage>2860</epage><pages>2853-2860</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>Dog serum and colostral immunoglobulin A (IgA) and free secretory component from colostrum were isolated using affinity chromatography. Both serum and colostral IgA showed similar susceptibility to reduction with dithiothreitol, but only colostral IgA released the additional subunit, bound secretory component. This released secretory component was identical with free secretory component with respect to electrophoretic migration, isoelectric focusing point, and molecular weight, but lacked some antigenic determinants. The amino acid composition and the N-terminal sequence of canine free secretory component was similar to that reported for the cow.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>807240</pmid><doi>10.1021/bi00684a010</doi><tpages>8</tpages></addata></record> |
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subjects | Amino Acids - analysis Animals Chromatography, Affinity Chromatography, Gel Colostrum - immunology Cross Reactions Dithiothreitol - pharmacology Dogs Electrophoresis, Polyacrylamide Gel Female Immunodiffusion Immunoelectrophoresis Immunoglobulin A - analysis Immunoglobulin A - isolation & purification Immunoglobulin A - metabolism Immunoglobulin Fragments - analysis Immunoglobulin Fragments - isolation & purification Immunoglobulin Fragments - metabolism Isoelectric Focusing Methods Molecular Weight Peptide Fragments - analysis Protein Binding Rabbits - immunology |
title | Structural composition of canine secretory component and immunoglobulin A |
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