A blood group A specific lectin from the seeds of Crotalaria striata.
A lectin, monospecific for human blood group A red blood cells was extracted from seeds of Crotalaria striata and purified by molecular sieving on Sephadex G-100 and ion-exchange on DEAE-cellulose. A molecular mass of 30 kDa was determined by SDS-polyacrylamide gel electrophoresis under non-reducing and reducing conditions. Molecular sieving on a Superose 12 column indicated a molecular mass of 110 kDa, suggesting the tetrameric nature of the native protein. Amino-acid composition showed the presence of aminated carbohydrate residues on the lectin. N-terminal amino-acid sequencing showed a striking similarity with the N-terminal sequence of the lectin from Crotalaria juncea, which is blood-group non-specific. The potency order of agglutination inhibition with galactose containing monosaccharides was N-acetyl-D-galactosamine greater than D-galactose greater than D-galactosamine as found for blood-group-A-specific lectins from other species.
Khang
N Q
NQ
Department of Biology, University of Hanoi, Vietnam.
Jean-Luc
G
G
Hoebeke
J
J
D000017:ABO Blood-Group System; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D037102:Lectins / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D037121:Plant Lectins; D012639:Seeds
D000017:ABO Blood-Group System; D000596:Amino Acids; D037102:Lectins; D037121:Plant Lectins