Lectins from seeds of Crotalaria pallida (smooth rattlebox).
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.
Rego
Evandro J L
EJ
UNEB-Departamento de Ciências, Campus II, Alagoinhas, BA, Brazil.
de Carvalho
Daniela D
DD
Marangoni
Sergio
S
de Oliveira
Benedito
B
Novello
José C
JC
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
D000596:Amino Acids; D037121:Plant Lectins