Purification and characterization of a lectin from Crotalaria paulina seeds.
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.
Pando
Luzia A
LA
Departamento de Bioquimica, Instituto de Biologia, Universidade Estadual de Campinas (UNICAMP), Campinas, SP, Brazil. luzpando@yahoo.com.br
de Carvalho
Daniela D
DD
Toyama
Marcos H
MH
Di Ciero
Luciana
L
Novello
José C
JC
Pascholatti
Sérgio F
SF
Marangoni
Sérgio
S
D000595:Amino Acid Sequence; D029864:Crotalaria / Q000737:chemistry*; D008969:Molecular Sequence Data; D037121:Plant Lectins / Q000032:analysis / Q000737:chemistry / Q000302:isolation & purification*; D012639:Seeds / Q000737:chemistry*
D037121:Plant Lectins