Isolation and characterization of a seed lectin from elderberry (Sambucus nigra L.) and its relationship to the bark lectins.
A third elderberry (Sambucus nigra L.) lectin (SNA-III) has been isolated from dry seeds by affinity chromatography on immobilized 2-acetamido-2-deoxy-D-galactose. This lectin is a blood-group, nonspecific glycoprotein containing 21% of carbohydrate, and is rich in asparagine (or aspartic acid), serine, glutamine (or glutamic acid), and glycine. Gel filtration on Superose 12 yielded a single symmetrical peak corresponding to mol. wt. 50,000, SDS-poly(acrylamide) gel (SDS-PAGE) electrophoresis showed a single polypeptide band of 33 kDa, indicating that the native protein is a dimer of identical subunits. Hapten-inhibition assays of the agglutination of red blood cells showed that 2-acetamido-2-deoxy-D-galactose is the best inhibitor, being twice as potent as D-galactose, melibiose, and 2-amino-2-deoxy-D-galactose. A comparison of SNA-III to the previously described elderberry-bark lectins, SNA-I and SNA-II, indicated that the seed lectin is well distinct from them.
Katholieke Universiteit Leuven, Fakulteit der Landbouwwetenschappen, Laboratorium voor Fytopathologie en Plantenbescherming, Belgium.
W J
WJ
Peumans
J T
JT
Kellens
A K
AK
Allen
E J
EJ
Van Damme
D000596:Amino Acids / Q000032:analysis; D050260:Carbohydrate Metabolism; D002241:Carbohydrates / Q000032:analysis; D006384:Hemagglutination; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007120:Immunochemistry; D037102:Lectins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D015394:Molecular Structure; D008970:Molecular Weight; D037121:Plant Lectins; D054788:Ribosome Inactivating Proteins; D012639:Seeds; D014197:Trees
D000596:Amino Acids; D002241:Carbohydrates; D037102:Lectins; D037121:Plant Lectins; C050600:Sambucus nigra lectins; D054788:Ribosome Inactivating Proteins