Purification and characterization of a Cytisus-type Ulex europeus hemagglutinin II by affinity chromatography.
Ulex europeus hemagglutinin II [Cytisus-type anti-H(O) hemagglutinin] inhibited most by di-N-acetylchitobiose has been purified by affinity chromatography on a column of chitobiose-Sepharose 4B, followed by gel filtration on Sephacryl S-300. The purified hemagglutinin was homogeneous by ultracentrifugal analysis and gave a single band by electrophoresis on polyacrylamide gel, and had a molecular weight of 105 000 by sedimentation equilibrium and an isoelectric point of pH 6.66. This hemagglutinin was found to be composed of four, apparently identical, subunits of a molecular weight of 25 000 +/- 2 000 by dodecyl sulphate-polyacrylamide gel electrophoresis, and to contain 10.3% carbohydrate in which mannose (3.7%) was the predominant sugar, with smaller amounts of glucose, glucosamine, xylose, fucose and galactose. Amino acid analysis of the purified hemagglutinin II showed a large amount of aspartic acid and serine, but as little as 0.1 mol/100 mol of cystine or methionine could be detected.
D000596:Amino Acids / Q000032:analysis; D002241:Carbohydrates / Q000032:analysis; D002846:Chromatography, Affinity / Q000379:methods; D006385:Hemagglutination Inhibition Tests; D006801:Humans; D008970:Molecular Weight; D010835:Phytohemagglutinins / Q000302:isolation & purification*; D037121:Plant Lectins; D012639:Seeds / Q000276:immunology*
D000596:Amino Acids; D002241:Carbohydrates; D010835:Phytohemagglutinins; D037121:Plant Lectins