Biochemical characterization of a lectin from Delonix regia seeds

dc.creatorPando, SC
dc.creatorMacedo, MLR
dc.creatorFreire, MGM
dc.creatorToyama, MH
dc.creatorNovello, JC
dc.creatorMarangoni, S
dc.date2002
dc.dateMAY
dc.date2014-11-15T04:39:40Z
dc.date2015-11-26T16:30:53Z
dc.date2014-11-15T04:39:40Z
dc.date2015-11-26T16:30:53Z
dc.date.accessioned2018-03-28T23:11:56Z
dc.date.available2018-03-28T23:11:56Z
dc.identifierJournal Of Protein Chemistry. Kluwer Academic/plenum Publ, v. 21, n. 4, n. 279, n. 285, 2002.
dc.identifier0277-8033
dc.identifierWOS:000177206600006
dc.identifier10.1023/A:1019797320348
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/55520
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/55520
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/55520
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1270074
dc.descriptionA lectin from Delonix regia (DRL) seeds was purified by gel filtration on Sephadex. G-100 followed by ion-exchange chromatography on diethylaminoethyl-Sepharose and reverse-phase high-performance liquid chromatography on a C18 column. Hemagglutinating activity was monitored using rat erythrocytes. DRL showed no specificity for human erythrocytes of ABO blood groups. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) revealed a single protein in the presence of 0.1 M of dithiothreitol (DTT) and in nonreducing. conditions. Native-PAGE showed that DRL is a monomer with a molecular mass of about 12 kDa, as determined by denaturing gel electrophoresis and gel filtration chromatography. An amino acid composition revealed the absence of cysteine residues, the presence of 1 mol methionine/mol protein and a high proportion of acidic amino acids and glycine. The N-terminal sequence of DRL was determined by Edman degradation, and up to 16 amino acid residues showed more than 90% homology with other lectins from the Leguminosae family. The optimal pH range for lectin activity was between pH 8.0 and 9.0, and the lectin was active up to 60degreesC. The lectin required Mn2+ for hemagglutinating activity and remained active after reduction with 0.1 M of DTT, but lost activity in the presence of 8 M of urea. Sodium metaperiodate had no effect on the activity of DRL.
dc.description21
dc.description4
dc.description279
dc.description285
dc.languageen
dc.publisherKluwer Academic/plenum Publ
dc.publisherNew York
dc.publisherEUA
dc.relationJournal Of Protein Chemistry
dc.relationJ. Protein Chem.
dc.rightsfechado
dc.sourceWeb of Science
dc.subjectDelonix regia
dc.subjectglucose/mannose lectin
dc.subjectLeguminosae seeds
dc.subjectN-terminal sequence
dc.subjectGalactoside-binding Lectin
dc.subjectAmino-acid-sequence
dc.subjectPlant-lectins
dc.subjectProteins
dc.subjectPurification
dc.subjectChromatography
dc.subjectRecognition
dc.subjectIsolectins
dc.subjectComplex
dc.titleBiochemical characterization of a lectin from Delonix regia seeds
dc.typeArtículos de revistas


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