Avidin binding of carboxyl-substituted biotin and analogs
The use of biotinylated hormones as ligands on avidin-Sepharose columns represents an attractive approach to the isolation of receptors. However, the strong noncovalent interaction between the hormone and its receptor on one hand and biotin and avidin on the other poses major obstacles to receptor r...
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| Veröffentlicht in: | Biochemistry (Easton) 1982-03, Vol.21 (5), p.978-984 |
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| container_end_page | 984 |
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| container_issue | 5 |
| container_start_page | 978 |
| container_title | Biochemistry (Easton) |
| container_volume | 21 |
| creator | Hofmann, Klaus Titus, Gail Montibeller, Judith A Finn, Frances M |
| description | The use of biotinylated hormones as ligands on avidin-Sepharose columns represents an attractive approach to the isolation of receptors. However, the strong noncovalent interaction between the hormone and its receptor on one hand and biotin and avidin on the other poses major obstacles to receptor retrieval. The authors report the results of a systematic search for weaker binding biotin containing ligands that are displaceable by biotin. The experiments indicate that the attachment of insulin to biotin or biotin analogues imposes a steric impediment to the interaction of the biotin residues with their avidin or succinoylavidin binding sites. The observation that insertion of a spacer between the avidin binding site and the insulin molecule increases the stability of the complexes supports this view. |
| doi_str_mv | 10.1021/bi00534a024 |
| format | Article |
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However, the strong noncovalent interaction between the hormone and its receptor on one hand and biotin and avidin on the other poses major obstacles to receptor retrieval. The authors report the results of a systematic search for weaker binding biotin containing ligands that are displaceable by biotin. The experiments indicate that the attachment of insulin to biotin or biotin analogues imposes a steric impediment to the interaction of the biotin residues with their avidin or succinoylavidin binding sites. The observation that insertion of a spacer between the avidin binding site and the insulin molecule increases the stability of the complexes supports this view.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi00534a024</identifier><identifier>PMID: 7041971</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>avidin ; Avidin - metabolism ; biotin ; Biotin - analogs & derivatives ; Biotin - metabolism ; Chromatography, Affinity - methods ; Insulin - analogs & derivatives ; Ovalbumin - analogs & derivatives ; Receptor, Insulin - isolation & purification ; Structure-Activity Relationship</subject><ispartof>Biochemistry (Easton), 1982-03, Vol.21 (5), p.978-984</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a451t-bc583d16578a47f3a1d36ce9fce7152b8c571311c01ce39b5b1a280a0a26863</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/bi00534a024$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi00534a024$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,2765,27076,27924,27925,56738,56788</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7041971$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hofmann, Klaus</creatorcontrib><creatorcontrib>Titus, Gail</creatorcontrib><creatorcontrib>Montibeller, Judith A</creatorcontrib><creatorcontrib>Finn, Frances M</creatorcontrib><title>Avidin binding of carboxyl-substituted biotin and analogs</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>The use of biotinylated hormones as ligands on avidin-Sepharose columns represents an attractive approach to the isolation of receptors. 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The observation that insertion of a spacer between the avidin binding site and the insulin molecule increases the stability of the complexes supports this view.</description><subject>avidin</subject><subject>Avidin - metabolism</subject><subject>biotin</subject><subject>Biotin - analogs & derivatives</subject><subject>Biotin - metabolism</subject><subject>Chromatography, Affinity - methods</subject><subject>Insulin - analogs & derivatives</subject><subject>Ovalbumin - analogs & derivatives</subject><subject>Receptor, Insulin - isolation & purification</subject><subject>Structure-Activity Relationship</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1982</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkM9LwzAUx4Moc05PnoWd9CDVlzZp2uMc_oKh4nbwFpI0HZldM5NWtv_ejI7hQfDweDy-H77fxxehcww3GGJ8Kw0ATYiAmBygPqYxRCTP6SHqA0AaxXkKx-jE-0U4CTDSQz0GBOcM91E--jaFqYfS1GHNh7YcKuGkXW-qyLfSN6ZpG10E3TYBE3URRlR27k_RUSkqr892e4CmD_ez8VM0eX18Ho8mkSAUN5FUNEsKnFKWCcLKROAiSZXOS6VZeFVmijKcYKwAK53kkkos4gwEiDjN0mSALjvXlbNfrfYNXxqvdFWJWtvWc0YgTlnyP4gpyUISBPC6A5Wz3jtd8pUzS-E2HAPf9sl_9Rnoi51tK5e62LO7AoMedbrxjV7vZeE-eXiLUT57m_KMkvHH3cs73_JXHS-U5wvbulCm_zP5BzM9ig0</recordid><startdate>19820302</startdate><enddate>19820302</enddate><creator>Hofmann, Klaus</creator><creator>Titus, Gail</creator><creator>Montibeller, Judith A</creator><creator>Finn, Frances M</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>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>19820302</creationdate><title>Avidin binding of carboxyl-substituted biotin and analogs</title><author>Hofmann, Klaus ; Titus, Gail ; Montibeller, Judith A ; Finn, Frances M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a451t-bc583d16578a47f3a1d36ce9fce7152b8c571311c01ce39b5b1a280a0a26863</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1982</creationdate><topic>avidin</topic><topic>Avidin - metabolism</topic><topic>biotin</topic><topic>Biotin - analogs & derivatives</topic><topic>Biotin - metabolism</topic><topic>Chromatography, Affinity - methods</topic><topic>Insulin - analogs & derivatives</topic><topic>Ovalbumin - analogs & derivatives</topic><topic>Receptor, Insulin - isolation & purification</topic><topic>Structure-Activity Relationship</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hofmann, Klaus</creatorcontrib><creatorcontrib>Titus, Gail</creatorcontrib><creatorcontrib>Montibeller, Judith A</creatorcontrib><creatorcontrib>Finn, Frances M</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hofmann, Klaus</au><au>Titus, Gail</au><au>Montibeller, Judith A</au><au>Finn, Frances M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Avidin binding of carboxyl-substituted biotin and analogs</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>1982-03-02</date><risdate>1982</risdate><volume>21</volume><issue>5</issue><spage>978</spage><epage>984</epage><pages>978-984</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>The use of biotinylated hormones as ligands on avidin-Sepharose columns represents an attractive approach to the isolation of receptors. However, the strong noncovalent interaction between the hormone and its receptor on one hand and biotin and avidin on the other poses major obstacles to receptor retrieval. The authors report the results of a systematic search for weaker binding biotin containing ligands that are displaceable by biotin. The experiments indicate that the attachment of insulin to biotin or biotin analogues imposes a steric impediment to the interaction of the biotin residues with their avidin or succinoylavidin binding sites. The observation that insertion of a spacer between the avidin binding site and the insulin molecule increases the stability of the complexes supports this view.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>7041971</pmid><doi>10.1021/bi00534a024</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-2960 |
| ispartof | Biochemistry (Easton), 1982-03, Vol.21 (5), p.978-984 |
| issn | 0006-2960 1520-4995 |
| language | eng |
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| source | MEDLINE; ACS Publications |
| subjects | avidin Avidin - metabolism biotin Biotin - analogs & derivatives Biotin - metabolism Chromatography, Affinity - methods Insulin - analogs & derivatives Ovalbumin - analogs & derivatives Receptor, Insulin - isolation & purification Structure-Activity Relationship |
| title | Avidin binding of carboxyl-substituted biotin and analogs |
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