Purification and characterization of a new type lactose-binding Ulex europaeus lectin by affinity chromatography.
A new type lactose-binding lectin was purified from extracts of Ulex europaeus seeds by affinity chromatography on a column of galactose-Sepharose 4B, followed by gel filtration on Sephacryl S-300. This lectin, designated as Ulex europaeus lectin III (UEA-III), was found to be inhibited by lactose. The dimeric lectin is a glycoprotein with a molecular mass of 70,000 Da; it consists of two apparently identical subunits of a molecular mass of 34,000 Da. Compositional analysis showed that this lectin contains 30% carbohydrate and a large amount of aspartic acid, serine and valine, but no sulfur-containing amino acids. The N-terminal amino-acid sequences of L-fucose-binding Ulex europaeus lectin I (UEA-I) and di-N-acetylchitobiose-binding Ulex europaeus lectin II (UEA-II), both of which we have already purified and characterized, and that of UEA-III were determined and compared.
Konami
Y
Y
Division of Chemical Toxicology and Immunochemistry, Faculty of Pharmaceutical Sciences, University of Tokyo.
Yamamoto
K
K
Osawa
T
T
D000595:Amino Acid Sequence; D002846:Chromatography, Affinity; D007785:Lactose / Q000378:metabolism*; D037102:Lectins / Q000737:chemistry / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D037121:Plant Lectins; D010944:Plants / Q000032:analysis*; D012639:Seeds / Q000032:analysis
D037102:Lectins; D037121:Plant Lectins; C036850:Ulex europaeus lectins; D007785:Lactose