Studies on a chitooligosaccharide-specific lectin from Coccinia indica. Thermodynamics and kinetics of umbelliferyl glycoside binding
Coccinia indica agglutinin (CIA) is a chitooligosaccharide-specific lectin with two binding sites/homodimer of Mr 32,000. Quenching studies implied tryptophan involvement in binding activity, which was confirmed by chemical modification experiments (A.R. Sanadi and A. Surolia, submitted for publicat...
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| Veröffentlicht in: | The Journal of biological chemistry 1994-02, Vol.269 (7), p.5072-5077 |
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| creator | Sanadi, A.R Surolia, A |
| description | Coccinia indica agglutinin (CIA) is a chitooligosaccharide-specific lectin with two binding sites/homodimer of Mr 32,000. Quenching studies implied tryptophan involvement in binding activity, which was confirmed by chemical modification experiments (A.R. Sanadi and A. Surolia, submitted for publication). Binding of 4-methylumbelliferyl chitooligosaccharides has been carried out to study their binding by CIA. Reversal experiments confirm the validity of the data previously obtained (A.R. Sanadi and A. Surolia, submitted for publication) from intrinsic fluorescence studies. Surprisingly, unlike wheat germ agglutinin, there is no consistent thermodynamic effect of the chromophoric label on binding activities as compared with the native sugars. From the changes in the optical properties of the chromophoric group upon binding to CIA, it has been possible to confirm that the tryptophan located in the binding site is closest to the fourth subsite. Thermodynamic analysis shows that the binding of the labeled tetrasaccharide is very strongly entropically driven, with the terminal, nonreducing sugar residue protruding from the binding pocket. The results of stopped-flow kinetic studies on the binding of the chromophoric trisaccharide by CIA show that the mechanism of binding is a one-step process |
| doi_str_mv | 10.1016/S0021-9258(17)37656-1 |
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Thermodynamics and kinetics of umbelliferyl glycoside binding</title><source>MEDLINE</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Alma/SFX Local Collection</source><creator>Sanadi, A.R ; Surolia, A</creator><creatorcontrib>Sanadi, A.R ; Surolia, A</creatorcontrib><description>Coccinia indica agglutinin (CIA) is a chitooligosaccharide-specific lectin with two binding sites/homodimer of Mr 32,000. Quenching studies implied tryptophan involvement in binding activity, which was confirmed by chemical modification experiments (A.R. Sanadi and A. Surolia, submitted for publication). Binding of 4-methylumbelliferyl chitooligosaccharides has been carried out to study their binding by CIA. Reversal experiments confirm the validity of the data previously obtained (A.R. Sanadi and A. Surolia, submitted for publication) from intrinsic fluorescence studies. Surprisingly, unlike wheat germ agglutinin, there is no consistent thermodynamic effect of the chromophoric label on binding activities as compared with the native sugars. From the changes in the optical properties of the chromophoric group upon binding to CIA, it has been possible to confirm that the tryptophan located in the binding site is closest to the fourth subsite. Thermodynamic analysis shows that the binding of the labeled tetrasaccharide is very strongly entropically driven, with the terminal, nonreducing sugar residue protruding from the binding pocket. The results of stopped-flow kinetic studies on the binding of the chromophoric trisaccharide by CIA show that the mechanism of binding is a one-step process</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(17)37656-1</identifier><identifier>PMID: 8106485</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>AMINOAZUCARES ; AMINOSUCRE ; Analytical, structural and metabolic biochemistry ; Binding, Competitive ; Biological and medical sciences ; Calorimetry ; Carbohydrate Sequence ; Chitin ; CUCURBITACEAE ; FISICA ; FLOEMA ; FRUITS ; FRUTAS ; Fundamental and applied biological sciences. Psychology ; Glycoproteins ; Glycosides - chemistry ; Kinetics ; LECTINA ; LECTINE ; Lectins - chemistry ; Mathematics ; Molecular Sequence Data ; OLIGOSACARIDOS ; OLIGOSACCHARIDE ; Oligosaccharides ; PHLOEME ; PHYSIQUE ; Plant Lectins ; Proteins ; Spectrometry, Fluorescence ; Thermodynamics ; TRIPTOFANO ; TRYPTOPHANE ; Umbelliferones</subject><ispartof>The Journal of biological chemistry, 1994-02, Vol.269 (7), p.5072-5077</ispartof><rights>1994 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c426t-d785f50e8c1947b8b2ea38b0d70655f0ddc63d1e17cfa1e5e442fb28aa06d4ed3</citedby><cites>FETCH-LOGICAL-c426t-d785f50e8c1947b8b2ea38b0d70655f0ddc63d1e17cfa1e5e442fb28aa06d4ed3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4042259$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8106485$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sanadi, A.R</creatorcontrib><creatorcontrib>Surolia, A</creatorcontrib><title>Studies on a chitooligosaccharide-specific lectin from Coccinia indica. Thermodynamics and kinetics of umbelliferyl glycoside binding</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Coccinia indica agglutinin (CIA) is a chitooligosaccharide-specific lectin with two binding sites/homodimer of Mr 32,000. Quenching studies implied tryptophan involvement in binding activity, which was confirmed by chemical modification experiments (A.R. Sanadi and A. Surolia, submitted for publication). Binding of 4-methylumbelliferyl chitooligosaccharides has been carried out to study their binding by CIA. Reversal experiments confirm the validity of the data previously obtained (A.R. Sanadi and A. Surolia, submitted for publication) from intrinsic fluorescence studies. Surprisingly, unlike wheat germ agglutinin, there is no consistent thermodynamic effect of the chromophoric label on binding activities as compared with the native sugars. From the changes in the optical properties of the chromophoric group upon binding to CIA, it has been possible to confirm that the tryptophan located in the binding site is closest to the fourth subsite. Thermodynamic analysis shows that the binding of the labeled tetrasaccharide is very strongly entropically driven, with the terminal, nonreducing sugar residue protruding from the binding pocket. The results of stopped-flow kinetic studies on the binding of the chromophoric trisaccharide by CIA show that the mechanism of binding is a one-step process</description><subject>AMINOAZUCARES</subject><subject>AMINOSUCRE</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Binding, Competitive</subject><subject>Biological and medical sciences</subject><subject>Calorimetry</subject><subject>Carbohydrate Sequence</subject><subject>Chitin</subject><subject>CUCURBITACEAE</subject><subject>FISICA</subject><subject>FLOEMA</subject><subject>FRUITS</subject><subject>FRUTAS</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glycoproteins</subject><subject>Glycosides - chemistry</subject><subject>Kinetics</subject><subject>LECTINA</subject><subject>LECTINE</subject><subject>Lectins - chemistry</subject><subject>Mathematics</subject><subject>Molecular Sequence Data</subject><subject>OLIGOSACARIDOS</subject><subject>OLIGOSACCHARIDE</subject><subject>Oligosaccharides</subject><subject>PHLOEME</subject><subject>PHYSIQUE</subject><subject>Plant Lectins</subject><subject>Proteins</subject><subject>Spectrometry, Fluorescence</subject><subject>Thermodynamics</subject><subject>TRIPTOFANO</subject><subject>TRYPTOPHANE</subject><subject>Umbelliferones</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kN2KFDEQhYMo67j6AsJCEBG96DVJJ-n0pQz-wYIXswvehXRSmY52J2PSjcwD-N527wxTN0VR3zlVHIRuKLmlhMqPO0IYrVom1HvafKgbKWRFn6ANJaquakF_PkWbC_IcvSjlF1mKt_QKXSlKJFdig_7tptkFKDhFbLDtw5TSEPapGGt7k4ODqhzABh8sHsBOIWKf04i3ydoQg8EhumDNLb7vIY_JHaMZgy3YRId_hwjTOiSP57GDYQge8nHA--FoU1m8cbfK4_4leubNUODVuV-jhy-f77ffqrsfX79vP91VljM5Va5RwgsCytKWN53qGJhadcQ1RArhiXNW1o4Cbaw3FARwznzHlDFEOg6uvkbvTr6HnP7MUCY9hmKXx0yENBfdyFq0rWILKE6gzamUDF4fchhNPmpK9Bq_foxfr9lq2ujH-DVddDfnA3M3gruoznkv-7fnvSnWDD6baEO5YJxwxkS7YG9OWB_2_d-QQXch2R5GzWSrGy1Is_74-gR5k7TZ58XnYdcKstzi9X_8DaQc</recordid><startdate>19940218</startdate><enddate>19940218</enddate><creator>Sanadi, A.R</creator><creator>Surolia, A</creator><general>American Society for Biochemistry and Molecular Biology</general><scope>FBQ</scope><scope>IQODW</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>19940218</creationdate><title>Studies on a chitooligosaccharide-specific lectin from Coccinia indica. Thermodynamics and kinetics of umbelliferyl glycoside binding</title><author>Sanadi, A.R ; Surolia, A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c426t-d785f50e8c1947b8b2ea38b0d70655f0ddc63d1e17cfa1e5e442fb28aa06d4ed3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>AMINOAZUCARES</topic><topic>AMINOSUCRE</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Binding, Competitive</topic><topic>Biological and medical sciences</topic><topic>Calorimetry</topic><topic>Carbohydrate Sequence</topic><topic>Chitin</topic><topic>CUCURBITACEAE</topic><topic>FISICA</topic><topic>FLOEMA</topic><topic>FRUITS</topic><topic>FRUTAS</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glycoproteins</topic><topic>Glycosides - chemistry</topic><topic>Kinetics</topic><topic>LECTINA</topic><topic>LECTINE</topic><topic>Lectins - chemistry</topic><topic>Mathematics</topic><topic>Molecular Sequence Data</topic><topic>OLIGOSACARIDOS</topic><topic>OLIGOSACCHARIDE</topic><topic>Oligosaccharides</topic><topic>PHLOEME</topic><topic>PHYSIQUE</topic><topic>Plant Lectins</topic><topic>Proteins</topic><topic>Spectrometry, Fluorescence</topic><topic>Thermodynamics</topic><topic>TRIPTOFANO</topic><topic>TRYPTOPHANE</topic><topic>Umbelliferones</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sanadi, A.R</creatorcontrib><creatorcontrib>Surolia, A</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</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>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sanadi, A.R</au><au>Surolia, A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Studies on a chitooligosaccharide-specific lectin from Coccinia indica. Thermodynamics and kinetics of umbelliferyl glycoside binding</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1994-02-18</date><risdate>1994</risdate><volume>269</volume><issue>7</issue><spage>5072</spage><epage>5077</epage><pages>5072-5077</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>Coccinia indica agglutinin (CIA) is a chitooligosaccharide-specific lectin with two binding sites/homodimer of Mr 32,000. Quenching studies implied tryptophan involvement in binding activity, which was confirmed by chemical modification experiments (A.R. Sanadi and A. Surolia, submitted for publication). Binding of 4-methylumbelliferyl chitooligosaccharides has been carried out to study their binding by CIA. Reversal experiments confirm the validity of the data previously obtained (A.R. Sanadi and A. Surolia, submitted for publication) from intrinsic fluorescence studies. Surprisingly, unlike wheat germ agglutinin, there is no consistent thermodynamic effect of the chromophoric label on binding activities as compared with the native sugars. From the changes in the optical properties of the chromophoric group upon binding to CIA, it has been possible to confirm that the tryptophan located in the binding site is closest to the fourth subsite. Thermodynamic analysis shows that the binding of the labeled tetrasaccharide is very strongly entropically driven, with the terminal, nonreducing sugar residue protruding from the binding pocket. The results of stopped-flow kinetic studies on the binding of the chromophoric trisaccharide by CIA show that the mechanism of binding is a one-step process</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>8106485</pmid><doi>10.1016/S0021-9258(17)37656-1</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | AMINOAZUCARES AMINOSUCRE Analytical, structural and metabolic biochemistry Binding, Competitive Biological and medical sciences Calorimetry Carbohydrate Sequence Chitin CUCURBITACEAE FISICA FLOEMA FRUITS FRUTAS Fundamental and applied biological sciences. Psychology Glycoproteins Glycosides - chemistry Kinetics LECTINA LECTINE Lectins - chemistry Mathematics Molecular Sequence Data OLIGOSACARIDOS OLIGOSACCHARIDE Oligosaccharides PHLOEME PHYSIQUE Plant Lectins Proteins Spectrometry, Fluorescence Thermodynamics TRIPTOFANO TRYPTOPHANE Umbelliferones |
| title | Studies on a chitooligosaccharide-specific lectin from Coccinia indica. Thermodynamics and kinetics of umbelliferyl glycoside binding |
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