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Characterization of cystic fibrosis factor and its interaction with human immunoglobulin
Cystic fibrosis factor activity (CFFA), assayed as the ability to stop oyster ciliary movement, was present in serum-free medium from actively growing cystic fibrosis skin fibroblast cultures. CFFA was associated with a low molecular weight, negatively charged molecule that contained no uronic acid...
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Published in: | The Journal of experimental medicine 1973-06, Vol.137 (6), p.1538-1543 |
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container_end_page | 1543 |
container_issue | 6 |
container_start_page | 1538 |
container_title | The Journal of experimental medicine |
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creator | Danes, B S Litwin, S D Hütteroth, T H Cleve, H Bearn, A G |
description | Cystic fibrosis factor activity (CFFA), assayed as the ability to stop oyster ciliary movement, was present in serum-free medium from actively growing cystic fibrosis skin fibroblast cultures. CFFA was associated with a low molecular weight, negatively charged molecule that contained no uronic acid and was heat and pH labile. When CFFA-positive media were mixed with human IgG1, the CFFA was chromatographically displaced and emerged with the IgG1 fraction on column chromatography. Experiments in which various immunoglobulins were added to CFFA-positive culture media and then incubated with specific anti-immunoglobulins suggested that CFFA binding was class specific for human IgG, subclass specific for IgG1 and IgG2, and occurred with intact unaggregated heavy chains but not with kappa- and lambda-light chains, or Fab, Fc, and F(ab')(2) fragments. The serum protein beta(2)-microglobulin, which has structural homology to IgG, also bound CFFA. |
doi_str_mv | 10.1084/jem.137.6.1538 |
format | article |
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CFFA was associated with a low molecular weight, negatively charged molecule that contained no uronic acid and was heat and pH labile. When CFFA-positive media were mixed with human IgG1, the CFFA was chromatographically displaced and emerged with the IgG1 fraction on column chromatography. Experiments in which various immunoglobulins were added to CFFA-positive culture media and then incubated with specific anti-immunoglobulins suggested that CFFA binding was class specific for human IgG, subclass specific for IgG1 and IgG2, and occurred with intact unaggregated heavy chains but not with kappa- and lambda-light chains, or Fab, Fc, and F(ab')(2) fragments. The serum protein beta(2)-microglobulin, which has structural homology to IgG, also bound CFFA.</description><identifier>ISSN: 0022-1007</identifier><identifier>EISSN: 1540-9538</identifier><identifier>DOI: 10.1084/jem.137.6.1538</identifier><identifier>PMID: 4709272</identifier><language>eng</language><publisher>United States: The Rockefeller University Press</publisher><subject>Age Factors ; Antigen-Antibody Reactions ; Brief Definitive Reports ; Cell Line ; Cells, Cultured ; Cystic Fibrosis - immunology ; Fibroblasts - analysis ; Fibroblasts - immunology ; Humans ; Immunoglobulin G - analysis ; Immunoglobulins - analysis ; Skin - immunology</subject><ispartof>The Journal of experimental medicine, 1973-06, Vol.137 (6), p.1538-1543</ispartof><rights>Copyright © 1973 by The Rockefeller University Press</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c385t-7728a7aa1bf4f621d1f06c2d5d31608719988f0dd579eaf8c99b8e4a9f4b48cc3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2139351/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2139351/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,315,733,786,790,891,27957,27958,53827,53829</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/4709272$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Danes, B S</creatorcontrib><creatorcontrib>Litwin, S D</creatorcontrib><creatorcontrib>Hütteroth, T H</creatorcontrib><creatorcontrib>Cleve, H</creatorcontrib><creatorcontrib>Bearn, A G</creatorcontrib><title>Characterization of cystic fibrosis factor and its interaction with human immunoglobulin</title><title>The Journal of experimental medicine</title><addtitle>J Exp Med</addtitle><description>Cystic fibrosis factor activity (CFFA), assayed as the ability to stop oyster ciliary movement, was present in serum-free medium from actively growing cystic fibrosis skin fibroblast cultures. CFFA was associated with a low molecular weight, negatively charged molecule that contained no uronic acid and was heat and pH labile. When CFFA-positive media were mixed with human IgG1, the CFFA was chromatographically displaced and emerged with the IgG1 fraction on column chromatography. Experiments in which various immunoglobulins were added to CFFA-positive culture media and then incubated with specific anti-immunoglobulins suggested that CFFA binding was class specific for human IgG, subclass specific for IgG1 and IgG2, and occurred with intact unaggregated heavy chains but not with kappa- and lambda-light chains, or Fab, Fc, and F(ab')(2) fragments. The serum protein beta(2)-microglobulin, which has structural homology to IgG, also bound CFFA.</description><subject>Age Factors</subject><subject>Antigen-Antibody Reactions</subject><subject>Brief Definitive Reports</subject><subject>Cell Line</subject><subject>Cells, Cultured</subject><subject>Cystic Fibrosis - immunology</subject><subject>Fibroblasts - analysis</subject><subject>Fibroblasts - immunology</subject><subject>Humans</subject><subject>Immunoglobulin G - analysis</subject><subject>Immunoglobulins - analysis</subject><subject>Skin - immunology</subject><issn>0022-1007</issn><issn>1540-9538</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1973</creationdate><recordtype>article</recordtype><recordid>eNpVkU1LxDAQhoMouq5evQk5eWtN0rRJLoIsfsGCFwVvIU0TN9Ima9Iq-uvNsovoaYaZZ94Z5gXgDKMSI04v38xQ4oqVTYnriu-BGa4pKkTO98EMIUIKjBA7AscpvSGEKa2bQ3BIGRKEkRl4WaxUVHo00X2r0QUPg4X6K41OQ-vaGJJL0GYgRKh8B92YoPMZz6UN_enGFVxNg_LQDcPkw2sf2ql3_gQcWNUnc7qLc_B8e_O0uC-Wj3cPi-tloStejwVjhCumFG4ttQ3BHbao0aSruwo3iDMsBOcWdV3NhFGWayFabqgSlraUa13NwdVWdz21g-m08WNUvVxHN6j4JYNy8n_Hu5V8DR-S4EpUNc4CFzuBGN4nk0Y5uKRN3ytvwpQkx4IgLngGyy2o81dSNPZ3CUZy44XMXsjshWzkxos8cP73tF989_zqB568iKM</recordid><startdate>19730601</startdate><enddate>19730601</enddate><creator>Danes, B S</creator><creator>Litwin, S D</creator><creator>Hütteroth, T H</creator><creator>Cleve, H</creator><creator>Bearn, A G</creator><general>The Rockefeller University Press</general><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><scope>5PM</scope></search><sort><creationdate>19730601</creationdate><title>Characterization of cystic fibrosis factor and its interaction with human immunoglobulin</title><author>Danes, B S ; Litwin, S D ; Hütteroth, T H ; Cleve, H ; Bearn, A G</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c385t-7728a7aa1bf4f621d1f06c2d5d31608719988f0dd579eaf8c99b8e4a9f4b48cc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1973</creationdate><topic>Age Factors</topic><topic>Antigen-Antibody Reactions</topic><topic>Brief Definitive Reports</topic><topic>Cell Line</topic><topic>Cells, Cultured</topic><topic>Cystic Fibrosis - immunology</topic><topic>Fibroblasts - analysis</topic><topic>Fibroblasts - immunology</topic><topic>Humans</topic><topic>Immunoglobulin G - analysis</topic><topic>Immunoglobulins - analysis</topic><topic>Skin - immunology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Danes, B S</creatorcontrib><creatorcontrib>Litwin, S D</creatorcontrib><creatorcontrib>Hütteroth, T H</creatorcontrib><creatorcontrib>Cleve, H</creatorcontrib><creatorcontrib>Bearn, A G</creatorcontrib><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><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of experimental medicine</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Danes, B S</au><au>Litwin, S D</au><au>Hütteroth, T H</au><au>Cleve, H</au><au>Bearn, A G</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of cystic fibrosis factor and its interaction with human immunoglobulin</atitle><jtitle>The Journal of experimental medicine</jtitle><addtitle>J Exp Med</addtitle><date>1973-06-01</date><risdate>1973</risdate><volume>137</volume><issue>6</issue><spage>1538</spage><epage>1543</epage><pages>1538-1543</pages><issn>0022-1007</issn><eissn>1540-9538</eissn><notes>ObjectType-Article-1</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-2</notes><notes>content type line 23</notes><abstract>Cystic fibrosis factor activity (CFFA), assayed as the ability to stop oyster ciliary movement, was present in serum-free medium from actively growing cystic fibrosis skin fibroblast cultures. CFFA was associated with a low molecular weight, negatively charged molecule that contained no uronic acid and was heat and pH labile. When CFFA-positive media were mixed with human IgG1, the CFFA was chromatographically displaced and emerged with the IgG1 fraction on column chromatography. Experiments in which various immunoglobulins were added to CFFA-positive culture media and then incubated with specific anti-immunoglobulins suggested that CFFA binding was class specific for human IgG, subclass specific for IgG1 and IgG2, and occurred with intact unaggregated heavy chains but not with kappa- and lambda-light chains, or Fab, Fc, and F(ab')(2) fragments. The serum protein beta(2)-microglobulin, which has structural homology to IgG, also bound CFFA.</abstract><cop>United States</cop><pub>The Rockefeller University Press</pub><pmid>4709272</pmid><doi>10.1084/jem.137.6.1538</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Age Factors Antigen-Antibody Reactions Brief Definitive Reports Cell Line Cells, Cultured Cystic Fibrosis - immunology Fibroblasts - analysis Fibroblasts - immunology Humans Immunoglobulin G - analysis Immunoglobulins - analysis Skin - immunology |
title | Characterization of cystic fibrosis factor and its interaction with human immunoglobulin |
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