A conformational change in concanavalin A detected by a calorimetric study of the binding of methyl α-D-mannopyranoside
The binding of methyl α-D-mannopyranoside to the lectin concanavalin A was studied by means of calorimetry. An apparent enthalpy of binding was also calculated from the variation of the equilibrium constant with temperature (van't Hoff ΔH). The ΔH measured directly was −30 to −38 kJ/mole indica...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1978-10, Vol.84 (3), p.684-690 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Munske, G.R. Magnuson, J.A. Krakauer, H. |
| description | The binding of methyl α-D-mannopyranoside to the lectin concanavalin A was studied by means of calorimetry. An apparent enthalpy of binding was also calculated from the variation of the equilibrium constant with temperature (van't Hoff ΔH). The ΔH measured directly was −30 to −38 kJ/mole indicating that the binding is driven by the ΔH change. In contrast, the van't Hoff ΔH was substantially smaller, about zero at pH 5.2. The difference in the ΔH measured directly and the van't Hoff ΔH implies that the conformation of concanavalin A undergoes a temperature dependent change at both pH's but most predominantly at pH 5.2. The existence of this conformational change was verified by difference absorption spectroscopy. |
| doi_str_mv | 10.1016/0006-291X(78)90759-3 |
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An apparent enthalpy of binding was also calculated from the variation of the equilibrium constant with temperature (van't Hoff ΔH). The ΔH measured directly was −30 to −38 kJ/mole indicating that the binding is driven by the ΔH change. In contrast, the van't Hoff ΔH was substantially smaller, about zero at pH 5.2. The difference in the ΔH measured directly and the van't Hoff ΔH implies that the conformation of concanavalin A undergoes a temperature dependent change at both pH's but most predominantly at pH 5.2. The existence of this conformational change was verified by difference absorption spectroscopy.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/0006-291X(78)90759-3</identifier><identifier>PMID: 718710</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Calorimetry ; Concanavalin A ; field crops ; Kinetics ; Methylglycosides ; Methylmannosides ; plant biochemistry ; plant physiology ; Protein Binding</subject><ispartof>Biochemical and biophysical research communications, 1978-10, Vol.84 (3), p.684-690</ispartof><rights>1978</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c380t-a526875cb692fc6d07c1168b453c59d19aef3a4cac1a17231914b3ff8d4df3e43</citedby><cites>FETCH-LOGICAL-c380t-a526875cb692fc6d07c1168b453c59d19aef3a4cac1a17231914b3ff8d4df3e43</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(78)90759-3$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>315,781,785,3551,27929,27930,46000</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/718710$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Munske, G.R.</creatorcontrib><creatorcontrib>Magnuson, J.A.</creatorcontrib><creatorcontrib>Krakauer, H.</creatorcontrib><title>A conformational change in concanavalin A detected by a calorimetric study of the binding of methyl α-D-mannopyranoside</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>The binding of methyl α-D-mannopyranoside to the lectin concanavalin A was studied by means of calorimetry. 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The existence of this conformational change was verified by difference absorption spectroscopy.</description><subject>Calorimetry</subject><subject>Concanavalin A</subject><subject>field crops</subject><subject>Kinetics</subject><subject>Methylglycosides</subject><subject>Methylmannosides</subject><subject>plant biochemistry</subject><subject>plant physiology</subject><subject>Protein Binding</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1978</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kM1u1TAQhS1EgdvCG1TCK1QWgXHsxMkG6aoFWqkSC6jEzpr4516jxL7YuRV5LF6EZyIhVZesRkfnzNHMR8g5g3cMWP0eAOqibNn3C9m8bUFWbcGfkA2DFoqSgXhKNo-RF-Q05x8AjIm6fU6eSdZIBhvya0t1DC6mAUcfA_ZU7zHsLPVhMTQGvMd-Fltq7Gj1aA3tJopUYx-TH-yYvKZ5PJqJRkfHvaWdD8aH3SJnez_19M_v4qoYMIR4mBKGmL2xL8mJwz7bVw_zjNx9-vjt8rq4_fL55nJ7W2jewFhgVdaNrHRXt6XTtQGpGaubTlRcV61hLVrHUWjUDJksOWuZ6LhzjRHGcSv4GXmz9h5S_Hm0eVSDz9r2PQYbj1lJUdYg5BIUa1CnmHOyTh3m_zBNioFaeKsFplpgKtmof7wVn9fOH_qP3WDN49IKeLZfr7bDqHCXfFZ3X0tgHEpRiwqWgg9rws4U7r1NKmtvg7bGp5m3MtH__4K__2Cakg</recordid><startdate>19781016</startdate><enddate>19781016</enddate><creator>Munske, G.R.</creator><creator>Magnuson, J.A.</creator><creator>Krakauer, H.</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>19781016</creationdate><title>A conformational change in concanavalin A detected by a calorimetric study of the binding of methyl α-D-mannopyranoside</title><author>Munske, G.R. ; Magnuson, J.A. ; Krakauer, H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c380t-a526875cb692fc6d07c1168b453c59d19aef3a4cac1a17231914b3ff8d4df3e43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1978</creationdate><topic>Calorimetry</topic><topic>Concanavalin A</topic><topic>field crops</topic><topic>Kinetics</topic><topic>Methylglycosides</topic><topic>Methylmannosides</topic><topic>plant biochemistry</topic><topic>plant physiology</topic><topic>Protein Binding</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Munske, G.R.</creatorcontrib><creatorcontrib>Magnuson, J.A.</creatorcontrib><creatorcontrib>Krakauer, H.</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>Munske, G.R.</au><au>Magnuson, J.A.</au><au>Krakauer, H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A conformational change in concanavalin A detected by a calorimetric study of the binding of methyl α-D-mannopyranoside</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1978-10-16</date><risdate>1978</risdate><volume>84</volume><issue>3</issue><spage>684</spage><epage>690</epage><pages>684-690</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>The binding of methyl α-D-mannopyranoside to the lectin concanavalin A was studied by means of calorimetry. An apparent enthalpy of binding was also calculated from the variation of the equilibrium constant with temperature (van't Hoff ΔH). The ΔH measured directly was −30 to −38 kJ/mole indicating that the binding is driven by the ΔH change. In contrast, the van't Hoff ΔH was substantially smaller, about zero at pH 5.2. The difference in the ΔH measured directly and the van't Hoff ΔH implies that the conformation of concanavalin A undergoes a temperature dependent change at both pH's but most predominantly at pH 5.2. The existence of this conformational change was verified by difference absorption spectroscopy.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>718710</pmid><doi>10.1016/0006-291X(78)90759-3</doi><tpages>7</tpages></addata></record> |
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| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | Calorimetry Concanavalin A field crops Kinetics Methylglycosides Methylmannosides plant biochemistry plant physiology Protein Binding |
| title | A conformational change in concanavalin A detected by a calorimetric study of the binding of methyl α-D-mannopyranoside |
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