Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/58446
Type: Artigo de periódico
Title: Purification and characterization of a lectin from Crotalaria paulina seeds
Author: Pando, LA
de Carvalho, DD
Toyama, MH
Di Ciero, L
Novello, JC
Pascholatti, SF
Marangoni, R
Abstract: A lectin was purified from Crotalaria paulina seeds by ion-exchange and FPLC molecular exclusion chromatography. CrpL had an apparent molecular mass of 30 kDa, as determined by SDS-PAGE under non-reducing and reducing conditions. CrpL effectively agglutinated human and cow erythrocytes, and this activity was not affected by 20 mM EDTA, showing no dependence of divalent cations. Hemagglutination was inhibited by N-acetyl-D-galactosamine, D-galactose and was also inhibited by glycoproteins, fetuin and asialofetuin. The N-terminal amino acid sequence of CrpL was identical to those of other lectins from the genus Crotalaria, and amino acid composition showed high amounts of Asx and Glx, and was rich in Gly, Ala and Ser, as also reported for lectins from other Crotalaria species. CrpL inhibited the growth of Xanthomonas axonopodis pv. phaseoli and Xanthomonas axonopodis pv. passiflorae, suggesting a role of this lectin in the defense of seeds against bacterial infections.
Subject: Crotalaria paulina
Leguminosae seeds
lectin
N-terminal sequence
Xanthomonas
Country: EUA
Editor: Kluwer Academic/plenum Publ
Rights: fechado
Identifier DOI: 10.1007/s10930-004-5219-9
Date Issue: 2004
Appears in Collections:Unicamp - Artigos e Outros Documentos

Files in This Item:
File Description SizeFormat 
WOS000225219900001.pdf264.72 kBAdobe PDFView/Open


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.