Purification and characterization of the major dog allergen, Can f I
Summary An important dog‐hair and dander‐specific allergen Ag13 has been purified by means of immunoaffinity chromatography utilizing rabbit antibody specific for Ag13. Purity was judged to be very high as detected by crossed immunoelectrophoresis and SDS‐PAGE. The purified allergen was subjected to...
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| Veröffentlicht in: | Clinical and experimental allergy 1991-05, Vol.21 (3), p.321-328 |
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| container_title | Clinical and experimental allergy |
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| creator | SCHOU, C. SVENDSEN, U. G. LøWENSTEIN, H. |
| description | Summary
An important dog‐hair and dander‐specific allergen Ag13 has been purified by means of immunoaffinity chromatography utilizing rabbit antibody specific for Ag13. Purity was judged to be very high as detected by crossed immunoelectrophoresis and SDS‐PAGE. The purified allergen was subjected to amino acid analyses. Molecular weight was about 22 kD in HPLC‐gel filtration and 25 kD in SDS PAGE with an additional band at 18 kD. In vitro IgE binding of the allergen was investigated by luminescence immunoassay (LIA) inhibition. Removal of Ag13 from dog hair and dander extract (DHD) removed 50 ± 1.5% of the IgE binding capacity. The purified allergen inhibited up to 56.5% of the IgE activity to DHD as measured with a pool of serum from dog‐allergic patients. Out of 26 dog‐allergic patients, 24 had a positive skin‐prick test to the allergen. Out of 23 dog‐allergic patients, 16 reacted with the allergen in IgE immunoblotting. We suggest that Ag13 be termed Can f I. The allergen will be a marker allergen for environmental dog hair and dander exposure. |
| doi_str_mv | 10.1111/j.1365-2222.1991.tb01663.x |
| format | Article |
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An important dog‐hair and dander‐specific allergen Ag13 has been purified by means of immunoaffinity chromatography utilizing rabbit antibody specific for Ag13. Purity was judged to be very high as detected by crossed immunoelectrophoresis and SDS‐PAGE. The purified allergen was subjected to amino acid analyses. Molecular weight was about 22 kD in HPLC‐gel filtration and 25 kD in SDS PAGE with an additional band at 18 kD. In vitro IgE binding of the allergen was investigated by luminescence immunoassay (LIA) inhibition. Removal of Ag13 from dog hair and dander extract (DHD) removed 50 ± 1.5% of the IgE binding capacity. The purified allergen inhibited up to 56.5% of the IgE activity to DHD as measured with a pool of serum from dog‐allergic patients. Out of 26 dog‐allergic patients, 24 had a positive skin‐prick test to the allergen. Out of 23 dog‐allergic patients, 16 reacted with the allergen in IgE immunoblotting. We suggest that Ag13 be termed Can f I. The allergen will be a marker allergen for environmental dog hair and dander exposure.</description><identifier>ISSN: 0954-7894</identifier><identifier>EISSN: 1365-2222</identifier><identifier>DOI: 10.1111/j.1365-2222.1991.tb01663.x</identifier><identifier>PMID: 1863894</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Allergens - immunology ; Amino Acid Sequence ; Animals ; Autoradiography ; Biological and medical sciences ; Dogs - immunology ; Humans ; Immunoblotting ; Immunoelectrophoresis, Two-Dimensional ; Immunoglobulin E - immunology ; Immunopathology ; Medical sciences ; Skin Tests</subject><ispartof>Clinical and experimental allergy, 1991-05, Vol.21 (3), p.321-328</ispartof><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3681-857df7c2917ba618e4766714b06c1eec90be400e339f232de675293c9bf2a79f3</citedby><cites>FETCH-LOGICAL-c3681-857df7c2917ba618e4766714b06c1eec90be400e339f232de675293c9bf2a79f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1365-2222.1991.tb01663.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1365-2222.1991.tb01663.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>315,782,786,1419,27931,27932,45581,45582</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5447339$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1863894$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>SCHOU, C.</creatorcontrib><creatorcontrib>SVENDSEN, U. G.</creatorcontrib><creatorcontrib>LøWENSTEIN, H.</creatorcontrib><title>Purification and characterization of the major dog allergen, Can f I</title><title>Clinical and experimental allergy</title><addtitle>Clin Exp Allergy</addtitle><description>Summary
An important dog‐hair and dander‐specific allergen Ag13 has been purified by means of immunoaffinity chromatography utilizing rabbit antibody specific for Ag13. Purity was judged to be very high as detected by crossed immunoelectrophoresis and SDS‐PAGE. The purified allergen was subjected to amino acid analyses. Molecular weight was about 22 kD in HPLC‐gel filtration and 25 kD in SDS PAGE with an additional band at 18 kD. In vitro IgE binding of the allergen was investigated by luminescence immunoassay (LIA) inhibition. Removal of Ag13 from dog hair and dander extract (DHD) removed 50 ± 1.5% of the IgE binding capacity. The purified allergen inhibited up to 56.5% of the IgE activity to DHD as measured with a pool of serum from dog‐allergic patients. Out of 26 dog‐allergic patients, 24 had a positive skin‐prick test to the allergen. Out of 23 dog‐allergic patients, 16 reacted with the allergen in IgE immunoblotting. We suggest that Ag13 be termed Can f I. The allergen will be a marker allergen for environmental dog hair and dander exposure.</description><subject>Allergens - immunology</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Autoradiography</subject><subject>Biological and medical sciences</subject><subject>Dogs - immunology</subject><subject>Humans</subject><subject>Immunoblotting</subject><subject>Immunoelectrophoresis, Two-Dimensional</subject><subject>Immunoglobulin E - immunology</subject><subject>Immunopathology</subject><subject>Medical sciences</subject><subject>Skin Tests</subject><issn>0954-7894</issn><issn>1365-2222</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkE9P4zAQxS20iC1_PgKStVpxIsGOEzveAxIq0CIh4ABC4mI5zhjcTROwU1H49LhKVc7MZaR5b549P4T-UJLSWCezlDJeJFmslEpJ074ilHOWLrfQaCP9QiMiizwRpcx_o90QZoQQVshyB-3QkrM4HqHzu4V31hndu67Fuq2xedFemx68-xyGncX9C-C5nnUe190z1k0D_hnaYzzWLbb4ah9tW90EOFj3PfRweXE_nibXt5Or8dl1YhgvaVIWorbCZJKKSnNaQi44FzSvCDcUwEhSQU4IMCZtxrIauCgyyYysbKaFtGwPHQ25r757W0Do1dwFA02jW-gWQZVEUCEKGY3_BqPxXQgerHr1bq79h6JErRCqmVpxUitOaoVQrRGqZVw-XL-yqOZQf68OzKL-d63rYHRjvW6NCxtbkeciXhBtp4Pt3TXw8YMPqPHFGctoDEiGABd6WG4CtP-vuGCiUI83EzW9eXpkk4yqKfsCr4abJA</recordid><startdate>199105</startdate><enddate>199105</enddate><creator>SCHOU, C.</creator><creator>SVENDSEN, U. G.</creator><creator>LøWENSTEIN, H.</creator><general>Blackwell Publishing Ltd</general><general>Blackwell</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>7X8</scope></search><sort><creationdate>199105</creationdate><title>Purification and characterization of the major dog allergen, Can f I</title><author>SCHOU, C. ; SVENDSEN, U. G. ; LøWENSTEIN, H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3681-857df7c2917ba618e4766714b06c1eec90be400e339f232de675293c9bf2a79f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Allergens - immunology</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Autoradiography</topic><topic>Biological and medical sciences</topic><topic>Dogs - immunology</topic><topic>Humans</topic><topic>Immunoblotting</topic><topic>Immunoelectrophoresis, Two-Dimensional</topic><topic>Immunoglobulin E - immunology</topic><topic>Immunopathology</topic><topic>Medical sciences</topic><topic>Skin Tests</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>SCHOU, C.</creatorcontrib><creatorcontrib>SVENDSEN, U. G.</creatorcontrib><creatorcontrib>LøWENSTEIN, H.</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>MEDLINE - Academic</collection><jtitle>Clinical and experimental allergy</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>SCHOU, C.</au><au>SVENDSEN, U. G.</au><au>LøWENSTEIN, H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and characterization of the major dog allergen, Can f I</atitle><jtitle>Clinical and experimental allergy</jtitle><addtitle>Clin Exp Allergy</addtitle><date>1991-05</date><risdate>1991</risdate><volume>21</volume><issue>3</issue><spage>321</spage><epage>328</epage><pages>321-328</pages><issn>0954-7894</issn><eissn>1365-2222</eissn><abstract>Summary
An important dog‐hair and dander‐specific allergen Ag13 has been purified by means of immunoaffinity chromatography utilizing rabbit antibody specific for Ag13. Purity was judged to be very high as detected by crossed immunoelectrophoresis and SDS‐PAGE. The purified allergen was subjected to amino acid analyses. Molecular weight was about 22 kD in HPLC‐gel filtration and 25 kD in SDS PAGE with an additional band at 18 kD. In vitro IgE binding of the allergen was investigated by luminescence immunoassay (LIA) inhibition. Removal of Ag13 from dog hair and dander extract (DHD) removed 50 ± 1.5% of the IgE binding capacity. The purified allergen inhibited up to 56.5% of the IgE activity to DHD as measured with a pool of serum from dog‐allergic patients. Out of 26 dog‐allergic patients, 24 had a positive skin‐prick test to the allergen. Out of 23 dog‐allergic patients, 16 reacted with the allergen in IgE immunoblotting. We suggest that Ag13 be termed Can f I. The allergen will be a marker allergen for environmental dog hair and dander exposure.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>1863894</pmid><doi>10.1111/j.1365-2222.1991.tb01663.x</doi><tpages>8</tpages></addata></record> |
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| ispartof | Clinical and experimental allergy, 1991-05, Vol.21 (3), p.321-328 |
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| subjects | Allergens - immunology Amino Acid Sequence Animals Autoradiography Biological and medical sciences Dogs - immunology Humans Immunoblotting Immunoelectrophoresis, Two-Dimensional Immunoglobulin E - immunology Immunopathology Medical sciences Skin Tests |
| title | Purification and characterization of the major dog allergen, Can f I |
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