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 > D-galactose > D-galactosamine as found for blood-group-A specific lectins from other species.

Nguyen Q.K., Guillaume J.-L., Hoebeke J.

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Từ khóa : lectin; amino acid sequence; article; blood group A; higher plant; nonhuman; plant; plant seed; priority journal; protein purification; ABO Blood-Group System; Amino Acid Sequence; Amino Acids; Electrophoresis, Polyacrylamide Gel; Human; Lectins; Molecular Sequence Data; Molecular Weight; Seeds; Support, Non-U.S. Gov't; Crotalaria juncea; Crotalaria pallida; Embryophyta; Spermatophyta