Polyacrylamide Gel Electrophoresis: Hormonal and Species Specificity Of Antibody Binding of Bovine I131 Thyrotropin.
Summary In polyacrylamide gel electro-phoresis of bovine I131-TSH the radioactivity and biological activity migrate similarly but with slight dissociation. Increasing quantities of antiserum shift increasing quantities of radioactivity to slower moving regions. Bovine TSH preparations interfere with...
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Veröffentlicht in: | Experimental biology and medicine (Maywood, N.J.) N.J.), 1966-07, Vol.122 (3), p.795-799 |
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container_title | Experimental biology and medicine (Maywood, N.J.) |
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creator | Heideman, M. Lawrence McGuire, William L. Levy, Richard P. Shipley, Reginald A. |
description | Summary
In polyacrylamide gel electro-phoresis of bovine I131-TSH the radioactivity and biological activity migrate similarly but with slight dissociation. Increasing quantities of antiserum shift increasing quantities of radioactivity to slower moving regions. Bovine TSH preparations interfere with I131-TSH binding to antibody in proportion to biological activity. Human TSH is much less active.
We thank Messrs. Frank Zodnik and Donald Eros for technical assistance; Drs. Robert W. Bates, Mary E. Carsten and John G. Pierce, and Peter G. Cond-liffe for supplying purified bovine TSH preparations. |
doi_str_mv | 10.3181/00379727-122-31254 |
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In polyacrylamide gel electro-phoresis of bovine I131-TSH the radioactivity and biological activity migrate similarly but with slight dissociation. Increasing quantities of antiserum shift increasing quantities of radioactivity to slower moving regions. Bovine TSH preparations interfere with I131-TSH binding to antibody in proportion to biological activity. Human TSH is much less active.
We thank Messrs. Frank Zodnik and Donald Eros for technical assistance; Drs. Robert W. Bates, Mary E. Carsten and John G. Pierce, and Peter G. Cond-liffe for supplying purified bovine TSH preparations.</description><identifier>ISSN: 0037-9727</identifier><identifier>ISSN: 1535-3702</identifier><identifier>EISSN: 1535-3699</identifier><identifier>DOI: 10.3181/00379727-122-31254</identifier><language>eng</language><publisher>London, England: SAGE Publications</publisher><ispartof>Experimental biology and medicine (Maywood, N.J.), 1966-07, Vol.122 (3), p.795-799</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>314,780,784,27922,27923</link.rule.ids></links><search><creatorcontrib>Heideman, M. Lawrence</creatorcontrib><creatorcontrib>McGuire, William L.</creatorcontrib><creatorcontrib>Levy, Richard P.</creatorcontrib><creatorcontrib>Shipley, Reginald A.</creatorcontrib><title>Polyacrylamide Gel Electrophoresis: Hormonal and Species Specificity Of Antibody Binding of Bovine I131 Thyrotropin.</title><title>Experimental biology and medicine (Maywood, N.J.)</title><description>Summary
In polyacrylamide gel electro-phoresis of bovine I131-TSH the radioactivity and biological activity migrate similarly but with slight dissociation. Increasing quantities of antiserum shift increasing quantities of radioactivity to slower moving regions. Bovine TSH preparations interfere with I131-TSH binding to antibody in proportion to biological activity. Human TSH is much less active.
We thank Messrs. Frank Zodnik and Donald Eros for technical assistance; Drs. Robert W. Bates, Mary E. Carsten and John G. Pierce, and Peter G. Cond-liffe for supplying purified bovine TSH preparations.</description><issn>0037-9727</issn><issn>1535-3702</issn><issn>1535-3699</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1966</creationdate><recordtype>article</recordtype><recordid>eNp9jz1PwzAURS0EEqHwB5gqdlM_v_hrRFVpkSrBALPlOC-QKiWVXYb8exIKK9Nd7rm6h7FbEPcIFhZCoHFGGg5ScgSpyjNWgELFUTt3zoqpwKfGJbvKeScEKCN1we5e-m4IMQ1d2Lc1zdfUzVcdxWPqDx99otzma3bRhC7TzW_O2Nvj6nW54dvn9dPyYcsjaHvkzlVBUaVQAtUQSwcWra0bAdIpIQxqXTtQgcooAoDTkdDUomp0KS26iDMmT7sx9TknavwhtfuQBg_CT5b-z9KPlv7HcoQWJyiHd_K7_it9jh__I74B4MxQ7w</recordid><startdate>196607</startdate><enddate>196607</enddate><creator>Heideman, M. Lawrence</creator><creator>McGuire, William L.</creator><creator>Levy, Richard P.</creator><creator>Shipley, Reginald A.</creator><general>SAGE Publications</general><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>196607</creationdate><title>Polyacrylamide Gel Electrophoresis</title><author>Heideman, M. Lawrence ; McGuire, William L. ; Levy, Richard P. ; Shipley, Reginald A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c168t-99ba5eb5321ed1c4918388df01295007366d915ae4c0a1196ce37d0bf642839c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1966</creationdate><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Heideman, M. Lawrence</creatorcontrib><creatorcontrib>McGuire, William L.</creatorcontrib><creatorcontrib>Levy, Richard P.</creatorcontrib><creatorcontrib>Shipley, Reginald A.</creatorcontrib><collection>CrossRef</collection><jtitle>Experimental biology and medicine (Maywood, N.J.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Heideman, M. Lawrence</au><au>McGuire, William L.</au><au>Levy, Richard P.</au><au>Shipley, Reginald A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Polyacrylamide Gel Electrophoresis: Hormonal and Species Specificity Of Antibody Binding of Bovine I131 Thyrotropin.</atitle><jtitle>Experimental biology and medicine (Maywood, N.J.)</jtitle><date>1966-07</date><risdate>1966</risdate><volume>122</volume><issue>3</issue><spage>795</spage><epage>799</epage><pages>795-799</pages><issn>0037-9727</issn><issn>1535-3702</issn><eissn>1535-3699</eissn><abstract>Summary
In polyacrylamide gel electro-phoresis of bovine I131-TSH the radioactivity and biological activity migrate similarly but with slight dissociation. Increasing quantities of antiserum shift increasing quantities of radioactivity to slower moving regions. Bovine TSH preparations interfere with I131-TSH binding to antibody in proportion to biological activity. Human TSH is much less active.
We thank Messrs. Frank Zodnik and Donald Eros for technical assistance; Drs. Robert W. Bates, Mary E. Carsten and John G. Pierce, and Peter G. Cond-liffe for supplying purified bovine TSH preparations.</abstract><cop>London, England</cop><pub>SAGE Publications</pub><doi>10.3181/00379727-122-31254</doi><tpages>5</tpages></addata></record> |
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source | Alma/SFX Local Collection |
title | Polyacrylamide Gel Electrophoresis: Hormonal and Species Specificity Of Antibody Binding of Bovine I131 Thyrotropin. |
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