A Co(III) derivative of concanavalin A
Co(III) has been stoichiometrically incorporated into jack bean concanavalin A. The Co(III) protein still possesses a binding site for an additional divalent transition metal ion which together with Ca(II) can induce the sugar binding ability. No H 2O 2 oxidation of Co(II) occurs with demetallized c...
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Veröffentlicht in: | Biochemical and biophysical research communications 1979-12, Vol.91 (3), p.1045-1050 |
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container_title | Biochemical and biophysical research communications |
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creator | Urdea, M.S. Christie, D.J. Munske, G.R. Magnuson, J.A. Legg, J.I. |
description | Co(III) has been stoichiometrically incorporated into jack bean concanavalin A. The Co(III) protein still possesses a binding site for an additional divalent transition metal ion which together with Ca(II) can induce the sugar binding ability. No H
2O
2 oxidation of Co(II) occurs with demetallized concanavalin A activated with Ca(II) and Co(II) unless Co(II) is present in a stoichiometric excess. Evidence is presented to indicate that kinetically stable Co(III) is bound to a completely different location than the thermodynamically stable Co(II) protein site. |
doi_str_mv | 10.1016/0006-291X(79)91985-5 |
format | Article |
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2O
2 oxidation of Co(II) occurs with demetallized concanavalin A activated with Ca(II) and Co(II) unless Co(II) is present in a stoichiometric excess. Evidence is presented to indicate that kinetically stable Co(III) is bound to a completely different location than the thermodynamically stable Co(II) protein site.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/0006-291X(79)91985-5</identifier><identifier>PMID: 526265</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Binding Sites ; Calcium ; Cobalt ; Concanavalin A ; Kinetics ; Nickel ; Protein Binding</subject><ispartof>Biochemical and biophysical research communications, 1979-12, Vol.91 (3), p.1045-1050</ispartof><rights>1979</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c380t-edc3b84c4f34be100b7382d0dc35297a0547edeba72d0374e0277905a8a7f4e13</citedby><cites>FETCH-LOGICAL-c380t-edc3b84c4f34be100b7382d0dc35297a0547edeba72d0374e0277905a8a7f4e13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0006-291X(79)91985-5$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>315,781,785,3551,27929,27930,46000</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/526265$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Urdea, M.S.</creatorcontrib><creatorcontrib>Christie, D.J.</creatorcontrib><creatorcontrib>Munske, G.R.</creatorcontrib><creatorcontrib>Magnuson, J.A.</creatorcontrib><creatorcontrib>Legg, J.I.</creatorcontrib><title>A Co(III) derivative of concanavalin A</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Co(III) has been stoichiometrically incorporated into jack bean concanavalin A. The Co(III) protein still possesses a binding site for an additional divalent transition metal ion which together with Ca(II) can induce the sugar binding ability. No H
2O
2 oxidation of Co(II) occurs with demetallized concanavalin A activated with Ca(II) and Co(II) unless Co(II) is present in a stoichiometric excess. Evidence is presented to indicate that kinetically stable Co(III) is bound to a completely different location than the thermodynamically stable Co(II) protein site.</description><subject>Binding Sites</subject><subject>Calcium</subject><subject>Cobalt</subject><subject>Concanavalin A</subject><subject>Kinetics</subject><subject>Nickel</subject><subject>Protein Binding</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1979</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kEtrwzAMgM3Yq-v2DwrLqbSHbLJjx_FlUMoehcIOW2E34zjK8GiTzm4L-_dzl9LjDkIgfRLSR8iAwh0Fmt8DQJ4yRT9GUo0VVYVIxQnpUVCQMgr8lPSOyCW5CuELgFKeqwtyLljOctEjw0kybUez2WycVOjdzmzcDpO2TmzbWNOYnVm6Jplck7PaLAPeHHKfLJ4e36cv6fz1eTadzFObFbBJsbJZWXDL64yXSAFKmRWsglgWTEkDgkussDQyFjPJEZiUCoQpjKw50qxPht3etW-_txg2euWCxeXSNNhug5a8ECIvWAR5B1rfhuCx1mvvVsb_aAp6b0fvX9f717VU-s-OFnFscNi_LVdYHYc6HbF927Vr02rz6V3QizcGNIPoU8WIxENHYLSwc-h1sA4bi5XzaDe6at3_F_wCFD16Aw</recordid><startdate>19791214</startdate><enddate>19791214</enddate><creator>Urdea, M.S.</creator><creator>Christie, D.J.</creator><creator>Munske, G.R.</creator><creator>Magnuson, J.A.</creator><creator>Legg, J.I.</creator><general>Elsevier Inc</general><scope>FBQ</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>19791214</creationdate><title>A Co(III) derivative of concanavalin A</title><author>Urdea, M.S. ; Christie, D.J. ; Munske, G.R. ; Magnuson, J.A. ; Legg, J.I.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c380t-edc3b84c4f34be100b7382d0dc35297a0547edeba72d0374e0277905a8a7f4e13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1979</creationdate><topic>Binding Sites</topic><topic>Calcium</topic><topic>Cobalt</topic><topic>Concanavalin A</topic><topic>Kinetics</topic><topic>Nickel</topic><topic>Protein Binding</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Urdea, M.S.</creatorcontrib><creatorcontrib>Christie, D.J.</creatorcontrib><creatorcontrib>Munske, G.R.</creatorcontrib><creatorcontrib>Magnuson, J.A.</creatorcontrib><creatorcontrib>Legg, J.I.</creatorcontrib><collection>AGRIS</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>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Urdea, M.S.</au><au>Christie, D.J.</au><au>Munske, G.R.</au><au>Magnuson, J.A.</au><au>Legg, J.I.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A Co(III) derivative of concanavalin A</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1979-12-14</date><risdate>1979</risdate><volume>91</volume><issue>3</issue><spage>1045</spage><epage>1050</epage><pages>1045-1050</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Co(III) has been stoichiometrically incorporated into jack bean concanavalin A. The Co(III) protein still possesses a binding site for an additional divalent transition metal ion which together with Ca(II) can induce the sugar binding ability. No H
2O
2 oxidation of Co(II) occurs with demetallized concanavalin A activated with Ca(II) and Co(II) unless Co(II) is present in a stoichiometric excess. Evidence is presented to indicate that kinetically stable Co(III) is bound to a completely different location than the thermodynamically stable Co(II) protein site.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>526265</pmid><doi>10.1016/0006-291X(79)91985-5</doi><tpages>6</tpages></addata></record> |
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language | eng |
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source | MEDLINE; Access via ScienceDirect (Elsevier) |
subjects | Binding Sites Calcium Cobalt Concanavalin A Kinetics Nickel Protein Binding |
title | A Co(III) derivative of concanavalin A |
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