Loading…

Avidin binding of biotinylated corticotropins

The authors studied the effect on avidin binding of attaching peptide hormones to biotin and biotin analogues. It is concluded that the attachment of ACTH sub(1-24) to biocytin amide and its analogues exerts little influence on the affinity for avidin or succinoylavidin, a result that differs marked...

Full description

Saved in:
Bibliographic Details
Published in:Biochemistry (Easton) 1983-02, Vol.22 (4), p.904-909
Main Authors: Romovacek, Hana, Finn, Frances M, Hofmann, Klaus
Format: Article
Language:English
Subjects:
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-a385t-1177df77a95dc2ff38d8013a0a3b79fbb75d1a54be9b7bf8348209d4e2995df83
cites
container_end_page 909
container_issue 4
container_start_page 904
container_title Biochemistry (Easton)
container_volume 22
creator Romovacek, Hana
Finn, Frances M
Hofmann, Klaus
description The authors studied the effect on avidin binding of attaching peptide hormones to biotin and biotin analogues. It is concluded that the attachment of ACTH sub(1-24) to biocytin amide and its analogues exerts little influence on the affinity for avidin or succinoylavidin, a result that differs markedly from that obtained with biotinylinsulin-succinoylavidin complexes. The attachment of insulin to biotin weakens significantly the avidin-biotin interaction presumably because the insulin molecular with its stable conformation exerts a steric impediment. Such an effect is not observed with the smaller, flexible biotinylated ACTH sub(1-24) molecules.
doi_str_mv 10.1021/bi00273a030
format article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_80439373</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>80439373</sourcerecordid><originalsourceid>FETCH-LOGICAL-a385t-1177df77a95dc2ff38d8013a0a3b79fbb75d1a54be9b7bf8348209d4e2995df83</originalsourceid><addsrcrecordid>eNqFkM1LAzEQxYMotX6cPAs96UFWJ5tks3usxapQsGA9h2STldTtpia7Yv97U7YUD4KHYebxfswMD6ELDLcYUnynLEDKiQQCB2iIWQoJLQp2iIYAkCVpkcExOglhGSUFTgdokBHAjMAQJeMvq20zUraJ7X3kqji61jabWrZGj0rnW1u61ru1bcIZOqpkHcz5rp-it-nDYvKUzF4enyfjWSJJztoEY851xbksmC7TqiK5zgHHByVRvKiU4kxjyagyheKqygnNUyg0NWl8W0d9iq76vWvvPjsTWrGyoTR1LRvjuiByoKQgnPwLYsYYppRG8KYHS-9C8KYSa29X0m8EBrFNUfxKMdKXu7WdWhm9Z3exRT_pfRta8723pf8QGSecicX8dVv4nk8nYh75656XZRBL1_kmpvfn5R-BsIcV</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>15551444</pqid></control><display><type>article</type><title>Avidin binding of biotinylated corticotropins</title><source>ACS CRKN Legacy Archives</source><creator>Romovacek, Hana ; Finn, Frances M ; Hofmann, Klaus</creator><creatorcontrib>Romovacek, Hana ; Finn, Frances M ; Hofmann, Klaus</creatorcontrib><description>The authors studied the effect on avidin binding of attaching peptide hormones to biotin and biotin analogues. It is concluded that the attachment of ACTH sub(1-24) to biocytin amide and its analogues exerts little influence on the affinity for avidin or succinoylavidin, a result that differs markedly from that obtained with biotinylinsulin-succinoylavidin complexes. The attachment of insulin to biotin weakens significantly the avidin-biotin interaction presumably because the insulin molecular with its stable conformation exerts a steric impediment. Such an effect is not observed with the smaller, flexible biotinylated ACTH sub(1-24) molecules.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi00273a030</identifier><identifier>PMID: 6301530</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Adrenocorticotropic Hormone - analogs &amp; derivatives ; Adrenocorticotropic Hormone - chemical synthesis ; Adrenocorticotropic Hormone - metabolism ; Amino Acid Sequence ; avidin ; Avidin - metabolism ; biotin ; Chromatography, High Pressure Liquid ; corticotropin ; Indicators and Reagents ; insulin ; Ovalbumin - analogs &amp; derivatives ; Protein Binding ; Structure-Activity Relationship</subject><ispartof>Biochemistry (Easton), 1983-02, Vol.22 (4), p.904-909</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a385t-1177df77a95dc2ff38d8013a0a3b79fbb75d1a54be9b7bf8348209d4e2995df83</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/bi00273a030$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi00273a030$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,27064,27924,27925,56766,56816</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6301530$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Romovacek, Hana</creatorcontrib><creatorcontrib>Finn, Frances M</creatorcontrib><creatorcontrib>Hofmann, Klaus</creatorcontrib><title>Avidin binding of biotinylated corticotropins</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>The authors studied the effect on avidin binding of attaching peptide hormones to biotin and biotin analogues. It is concluded that the attachment of ACTH sub(1-24) to biocytin amide and its analogues exerts little influence on the affinity for avidin or succinoylavidin, a result that differs markedly from that obtained with biotinylinsulin-succinoylavidin complexes. The attachment of insulin to biotin weakens significantly the avidin-biotin interaction presumably because the insulin molecular with its stable conformation exerts a steric impediment. Such an effect is not observed with the smaller, flexible biotinylated ACTH sub(1-24) molecules.</description><subject>Adrenocorticotropic Hormone - analogs &amp; derivatives</subject><subject>Adrenocorticotropic Hormone - chemical synthesis</subject><subject>Adrenocorticotropic Hormone - metabolism</subject><subject>Amino Acid Sequence</subject><subject>avidin</subject><subject>Avidin - metabolism</subject><subject>biotin</subject><subject>Chromatography, High Pressure Liquid</subject><subject>corticotropin</subject><subject>Indicators and Reagents</subject><subject>insulin</subject><subject>Ovalbumin - analogs &amp; derivatives</subject><subject>Protein Binding</subject><subject>Structure-Activity Relationship</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1983</creationdate><recordtype>article</recordtype><recordid>eNqFkM1LAzEQxYMotX6cPAs96UFWJ5tks3usxapQsGA9h2STldTtpia7Yv97U7YUD4KHYebxfswMD6ELDLcYUnynLEDKiQQCB2iIWQoJLQp2iIYAkCVpkcExOglhGSUFTgdokBHAjMAQJeMvq20zUraJ7X3kqji61jabWrZGj0rnW1u61ru1bcIZOqpkHcz5rp-it-nDYvKUzF4enyfjWSJJztoEY851xbksmC7TqiK5zgHHByVRvKiU4kxjyagyheKqygnNUyg0NWl8W0d9iq76vWvvPjsTWrGyoTR1LRvjuiByoKQgnPwLYsYYppRG8KYHS-9C8KYSa29X0m8EBrFNUfxKMdKXu7WdWhm9Z3exRT_pfRta8723pf8QGSecicX8dVv4nk8nYh75656XZRBL1_kmpvfn5R-BsIcV</recordid><startdate>19830215</startdate><enddate>19830215</enddate><creator>Romovacek, Hana</creator><creator>Finn, Frances M</creator><creator>Hofmann, Klaus</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>19830215</creationdate><title>Avidin binding of biotinylated corticotropins</title><author>Romovacek, Hana ; Finn, Frances M ; Hofmann, Klaus</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a385t-1177df77a95dc2ff38d8013a0a3b79fbb75d1a54be9b7bf8348209d4e2995df83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1983</creationdate><topic>Adrenocorticotropic Hormone - analogs &amp; derivatives</topic><topic>Adrenocorticotropic Hormone - chemical synthesis</topic><topic>Adrenocorticotropic Hormone - metabolism</topic><topic>Amino Acid Sequence</topic><topic>avidin</topic><topic>Avidin - metabolism</topic><topic>biotin</topic><topic>Chromatography, High Pressure Liquid</topic><topic>corticotropin</topic><topic>Indicators and Reagents</topic><topic>insulin</topic><topic>Ovalbumin - analogs &amp; derivatives</topic><topic>Protein Binding</topic><topic>Structure-Activity Relationship</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Romovacek, Hana</creatorcontrib><creatorcontrib>Finn, Frances M</creatorcontrib><creatorcontrib>Hofmann, Klaus</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>Romovacek, Hana</au><au>Finn, Frances M</au><au>Hofmann, Klaus</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Avidin binding of biotinylated corticotropins</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>1983-02-15</date><risdate>1983</risdate><volume>22</volume><issue>4</issue><spage>904</spage><epage>909</epage><pages>904-909</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>The authors studied the effect on avidin binding of attaching peptide hormones to biotin and biotin analogues. It is concluded that the attachment of ACTH sub(1-24) to biocytin amide and its analogues exerts little influence on the affinity for avidin or succinoylavidin, a result that differs markedly from that obtained with biotinylinsulin-succinoylavidin complexes. The attachment of insulin to biotin weakens significantly the avidin-biotin interaction presumably because the insulin molecular with its stable conformation exerts a steric impediment. Such an effect is not observed with the smaller, flexible biotinylated ACTH sub(1-24) molecules.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>6301530</pmid><doi>10.1021/bi00273a030</doi><tpages>6</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0006-2960
ispartof Biochemistry (Easton), 1983-02, Vol.22 (4), p.904-909
issn 0006-2960
1520-4995
language eng
recordid cdi_proquest_miscellaneous_80439373
source ACS CRKN Legacy Archives
subjects Adrenocorticotropic Hormone - analogs & derivatives
Adrenocorticotropic Hormone - chemical synthesis
Adrenocorticotropic Hormone - metabolism
Amino Acid Sequence
avidin
Avidin - metabolism
biotin
Chromatography, High Pressure Liquid
corticotropin
Indicators and Reagents
insulin
Ovalbumin - analogs & derivatives
Protein Binding
Structure-Activity Relationship
title Avidin binding of biotinylated corticotropins
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-05T10%3A53%3A37IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Avidin%20binding%20of%20biotinylated%20corticotropins&rft.jtitle=Biochemistry%20(Easton)&rft.au=Romovacek,%20Hana&rft.date=1983-02-15&rft.volume=22&rft.issue=4&rft.spage=904&rft.epage=909&rft.pages=904-909&rft.issn=0006-2960&rft.eissn=1520-4995&rft_id=info:doi/10.1021/bi00273a030&rft_dat=%3Cproquest_cross%3E80439373%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-a385t-1177df77a95dc2ff38d8013a0a3b79fbb75d1a54be9b7bf8348209d4e2995df83%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=15551444&rft_id=info:pmid/6301530&rfr_iscdi=true