title: Lectins from seeds of Crotalaria pallida (smooth rattlebox).
abstract: A lectin from the seeds of Crotalaria pallida (CPL), with an apparent molecular mass of 30 kDa, determined by SDS-polyacrylamide gel electrophoresis, showed human type A and B erythrocytes agglutination activity, which is inhibited by raffinose and galactose. The lectin requirement for divalent cation was demonstrated with EDTA/EGTA blocking hemagglutination activity. Although the N-terminal amino acid sequence of CPL is identical to another lectin from Crotalaria striata, which is taxonomically synonymous to Crotalaria pallida, these lectins differ in amino acid composition and hemagglutination properties.
authors.affiliation: UNEB-Departamento de Ciências, Campus II, Alagoinhas, BA, Brazil.
authors.forename: Evandro J L
authors.initials: EJ
authors.lastname: Rego
authors.forename: Daniela D
authors.initials: DD
authors.lastname: de Carvalho
authors.forename: Sergio
authors.initials: S
authors.lastname: Marangoni
authors.forename: Benedito
authors.initials: B
authors.lastname: de Oliveira
authors.forename: José C
authors.initials: JC
authors.lastname: Novello
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D029864:Crotalaria / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D004912:Erythrocytes / Q000187:drug effects; D006384:Hemagglutination / Q000187:drug effects; D006801:Humans; D008970:Molecular Weight; D037121:Plant Lectins / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D012639:Seeds / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid; D013552:Swine
chemical_list: D000596:Amino Acids; D037121:Plant Lectins