Galactose oxidase. An enzyme with lectin properties.
Galactose oxidase interacts with immobilized D-galactosyl residues and related immobilized and free sugars under the conditions of affinity electrophoresis in polyacrylamide gel and agglutinates sialidase-treated human erythrocytes. The agglutination is also inhibited by D-galactose and its derivatives and is temperature dependent. The sugar binding and hemagglutinating activity are preserved after removal of Cu2+ essential for enzymic activity. These properties are very similar to those of some typical lectins; however, a number of D-galactose specific lectins do not possess any detectable galactose oxidase activity.
D050260:Carbohydrate Metabolism; D055598:Chemical Phenomena; D002621:Chemistry; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D005692:Galactose Oxidase / Q000378:metabolism; D037102:Lectins
D037102:Lectins; D005692:Galactose Oxidase