Purification and characterization of N-acetyl-D-galactosamine-binding lectin from Falcata japonica.
An N-acetyl-D-galactosamine-binding lectin from Falcata japonica seeds was purified by affinity column chromatography of N-acetyl-D-galactosamine coupled to epoxy-activated Sepharose 6B. A 1000-fold purification of lectin was obtained from the crude extracts. The purified lectin agglutinated blood group A red cells, but neither blood group B nor O red cells. Polyacrylamide gel electrophoresis of the lectin showed one diffuse band. Molecular weights of 125,000 and 117,000 were estimated by gel filtration and ultracentrifugal analysis, respectively. SDS-polyacrylamide gel electrophoresis of the lectin also showed a single band which has a molecular weight of 34,000. Therefore, the lectin molecule was estimated to be a tetramer composed of four identical non-covalently bound subunits. F. japonica lectin was a glycoprotein containing 5% total carbohydrate, and the amino acid composition was characterized by a high content of aspartic acid, serine and glycine, a low content of methionine and the absence of cysteine.
Nakajima
T
T
Department of Legal Medicine, Gunma University School of Medicine, Maebashi, Japan.
Yazawa
S
S
Kogure
T
T
Furukawa
K
K
D000017:ABO Blood-Group System; D000116:Acetylgalactosamine; D000596:Amino Acids / Q000032:analysis; D002241:Carbohydrates / Q000032:analysis; D002846:Chromatography, Affinity; D005688:Galactosamine / Q000031:analogs & derivatives; D006386:Hemagglutination Tests; D006801:Humans; D037102:Lectins / Q000302:isolation & purification*; D008970:Molecular Weight; D037121:Plant Lectins
D000017:ABO Blood-Group System; D000596:Amino Acids; D002241:Carbohydrates; C055007:Falcata lectin; D037102:Lectins; D037121:Plant Lectins; D005688:Galactosamine; D000116:Acetylgalactosamine