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Detection, Quantitation, and Characterization of the Major Internal Virion Antigen of the Bovine Leukemia Virus by Radioimmunoassay
The major internal polypeptide of the bovine leukemia virus (BLV) was purified to homogeneity with the use of gel filtration and affinity chromatography. Like previous results, the protein had a molecular weight of 25,000 daltons as determined by electrophoresis in polyacrylamide gels with sodium do...
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Published in: | JNCI : Journal of the National Cancer Institute 1976-10, Vol.57 (4), p.875-882 |
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description | The major internal polypeptide of the bovine leukemia virus (BLV) was purified to homogeneity with the use of gel filtration and affinity chromatography. Like previous results, the protein had a molecular weight of 25,000 daltons as determined by electrophoresis in polyacrylamide gels with sodium dodecyl sulfate, More than 90% of the 125I-labeled protein was precipitated by bovine sera that reacted in immunofluorescence tests with acetone-fixed BLV-infected cells. In contrast, minimal precipitation ( |
doi_str_mv | 10.1093/jnci/57.4.875 |
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Like previous results, the protein had a molecular weight of 25,000 daltons as determined by electrophoresis in polyacrylamide gels with sodium dodecyl sulfate, More than 90% of the 125I-labeled protein was precipitated by bovine sera that reacted in immunofluorescence tests with acetone-fixed BLV-infected cells. In contrast, minimal precipitation (<5%) was observed with sera from 36 cattle in leukemia-free herds; these sera, negative by immunofluorescence, included six samples that had high titers of antibodies to the foamy-like bovine syncytia virus (BSV). Antisera prepared against several other oncornaviruses or the Mason-Pfizer monkey virus (M-PMV) did not bind the BLV p25 protein. Conversely, the labeled p30 polypeptides of several oncornaviruses tested did not react with bovine sera that had high titers of antibodies to BLV p25. Competitive radioimmunoassay(s) (RIA) also failed to detect cross-reactions between BLV p25 protein and the internal polypeptides of other mammalian and' avian oncornaviruses, M-PMV, or foamy-like BSV. The RIA for BLV p25 antigen was also highly sensitive and specific for the detection and quantitation of the antigen in virus preparations and cell homogenates.</description><identifier>ISSN: 0027-8874</identifier><identifier>EISSN: 1460-2105</identifier><identifier>DOI: 10.1093/jnci/57.4.875</identifier><identifier>PMID: 63563</identifier><language>eng</language><publisher>United States: Oxford University Press</publisher><subject>Animals ; Antigens, Viral - analysis ; Binding, Competitive ; Cattle ; Cell Line ; Epitopes ; Leukemia Virus, Bovine - immunology ; Molecular Weight ; Radioimmunoassay ; Retroviridae - immunology ; Viral Proteins - analysis ; Viral Proteins - immunology</subject><ispartof>JNCI : Journal of the National Cancer Institute, 1976-10, Vol.57 (4), p.875-882</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/63563$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>McDonald, Hugh C.</creatorcontrib><creatorcontrib>Ferrer, Jorge F.</creatorcontrib><title>Detection, Quantitation, and Characterization of the Major Internal Virion Antigen of the Bovine Leukemia Virus by Radioimmunoassay</title><title>JNCI : Journal of the National Cancer Institute</title><addtitle>Journal of the National Cancer Institute</addtitle><description>The major internal polypeptide of the bovine leukemia virus (BLV) was purified to homogeneity with the use of gel filtration and affinity chromatography. Like previous results, the protein had a molecular weight of 25,000 daltons as determined by electrophoresis in polyacrylamide gels with sodium dodecyl sulfate, More than 90% of the 125I-labeled protein was precipitated by bovine sera that reacted in immunofluorescence tests with acetone-fixed BLV-infected cells. In contrast, minimal precipitation (<5%) was observed with sera from 36 cattle in leukemia-free herds; these sera, negative by immunofluorescence, included six samples that had high titers of antibodies to the foamy-like bovine syncytia virus (BSV). Antisera prepared against several other oncornaviruses or the Mason-Pfizer monkey virus (M-PMV) did not bind the BLV p25 protein. Conversely, the labeled p30 polypeptides of several oncornaviruses tested did not react with bovine sera that had high titers of antibodies to BLV p25. Competitive radioimmunoassay(s) (RIA) also failed to detect cross-reactions between BLV p25 protein and the internal polypeptides of other mammalian and' avian oncornaviruses, M-PMV, or foamy-like BSV. The RIA for BLV p25 antigen was also highly sensitive and specific for the detection and quantitation of the antigen in virus preparations and cell homogenates.</description><subject>Animals</subject><subject>Antigens, Viral - analysis</subject><subject>Binding, Competitive</subject><subject>Cattle</subject><subject>Cell Line</subject><subject>Epitopes</subject><subject>Leukemia Virus, Bovine - immunology</subject><subject>Molecular Weight</subject><subject>Radioimmunoassay</subject><subject>Retroviridae - immunology</subject><subject>Viral Proteins - analysis</subject><subject>Viral Proteins - immunology</subject><issn>0027-8874</issn><issn>1460-2105</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1976</creationdate><recordtype>article</recordtype><recordid>eNo9kDtPwzAQgC1EBeUxMrF4YiLFSew4GaHlUamAqAAhlujiXKjbximxgygrf5z0Ibzc4_vupDMhJz7r-SwJL6ZG6Qshe7wXS7FDuj6PmBf4TOySLmOB9OJY8n1yYO2UtS8J-B7pRKGIwi75HaBD5XRlzulTA8ZpB5sKTE77E6hBOaz1z7pLq4K6CdJ7mFY1HZqWGJjTV12v4GU7_YH_0lX1pQ3SETYzLDWsrMbSbEnHkOtKl2VjKrAWlkekU8Dc4vE2HpKXm-vn_p03erwd9i9Hng544LwswSAWASiWiQIzCZmKAwbAZALtyTLPc4lJoXLhKx5HhQJRZCh8HkoUnEN4SM42exd19dmgdWmprcL5HAxWjU3jULJI-FErnm7FJisxTxe1LqFepus_a6m3odo6_P6HUM_SSIZSpHdv76l4GA_aXKQ8_AOxn3_F</recordid><startdate>197610</startdate><enddate>197610</enddate><creator>McDonald, Hugh C.</creator><creator>Ferrer, Jorge F.</creator><general>Oxford University Press</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>197610</creationdate><title>Detection, Quantitation, and Characterization of the Major Internal Virion Antigen of the Bovine Leukemia Virus by Radioimmunoassay</title><author>McDonald, Hugh C. ; Ferrer, Jorge F.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-i242t-b9e2852ac0b5feb7abc820aa079a1467ddd7e9fcd51c486fca5fbe51437e544a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1976</creationdate><topic>Animals</topic><topic>Antigens, Viral - analysis</topic><topic>Binding, Competitive</topic><topic>Cattle</topic><topic>Cell Line</topic><topic>Epitopes</topic><topic>Leukemia Virus, Bovine - immunology</topic><topic>Molecular Weight</topic><topic>Radioimmunoassay</topic><topic>Retroviridae - immunology</topic><topic>Viral Proteins - analysis</topic><topic>Viral Proteins - immunology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>McDonald, Hugh C.</creatorcontrib><creatorcontrib>Ferrer, Jorge F.</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>JNCI : Journal of the National Cancer Institute</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>McDonald, Hugh C.</au><au>Ferrer, Jorge F.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Detection, Quantitation, and Characterization of the Major Internal Virion Antigen of the Bovine Leukemia Virus by Radioimmunoassay</atitle><jtitle>JNCI : Journal of the National Cancer Institute</jtitle><addtitle>Journal of the National Cancer Institute</addtitle><date>1976-10</date><risdate>1976</risdate><volume>57</volume><issue>4</issue><spage>875</spage><epage>882</epage><pages>875-882</pages><issn>0027-8874</issn><eissn>1460-2105</eissn><abstract>The major internal polypeptide of the bovine leukemia virus (BLV) was purified to homogeneity with the use of gel filtration and affinity chromatography. Like previous results, the protein had a molecular weight of 25,000 daltons as determined by electrophoresis in polyacrylamide gels with sodium dodecyl sulfate, More than 90% of the 125I-labeled protein was precipitated by bovine sera that reacted in immunofluorescence tests with acetone-fixed BLV-infected cells. In contrast, minimal precipitation (<5%) was observed with sera from 36 cattle in leukemia-free herds; these sera, negative by immunofluorescence, included six samples that had high titers of antibodies to the foamy-like bovine syncytia virus (BSV). Antisera prepared against several other oncornaviruses or the Mason-Pfizer monkey virus (M-PMV) did not bind the BLV p25 protein. Conversely, the labeled p30 polypeptides of several oncornaviruses tested did not react with bovine sera that had high titers of antibodies to BLV p25. Competitive radioimmunoassay(s) (RIA) also failed to detect cross-reactions between BLV p25 protein and the internal polypeptides of other mammalian and' avian oncornaviruses, M-PMV, or foamy-like BSV. The RIA for BLV p25 antigen was also highly sensitive and specific for the detection and quantitation of the antigen in virus preparations and cell homogenates.</abstract><cop>United States</cop><pub>Oxford University Press</pub><pmid>63563</pmid><doi>10.1093/jnci/57.4.875</doi><tpages>8</tpages></addata></record> |
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source | Oxford University Press:Jisc Collections:Oxford Journal Archive: Access period 2024-2025 |
subjects | Animals Antigens, Viral - analysis Binding, Competitive Cattle Cell Line Epitopes Leukemia Virus, Bovine - immunology Molecular Weight Radioimmunoassay Retroviridae - immunology Viral Proteins - analysis Viral Proteins - immunology |
title | Detection, Quantitation, and Characterization of the Major Internal Virion Antigen of the Bovine Leukemia Virus by Radioimmunoassay |
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