The glycoprotein nature of phospholipase A2, hyaluronidase and acid phosphatase from honey-bee venom.
Experiments with immobilized concanavalin A strongly suggest a glycoprotein nature of three honey-bee venom enzymes, phospholipase A2, hyaluronidase and acid phosphatase. The electrophoretically and chromatographically detectable heterogeneity of phospholipase A2 results from absence of carbohydrate in a subfraction. Mannose, fucose and N-acetylglucosamine, but not galactose nor N-acetylgalactosamine, are present in the con A-binding fraction of bee venom. It is therefore concluded that only N-glycosidically linked carbohydrate occurs in bee venom glycoproteins.
D000135:Acid Phosphatase / Q000032:analysis*; D000818:Animals; D001514:Bee Venoms / Q000032:analysis*; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006023:Glycoproteins / Q000032:analysis*; D006821:Hyaluronoglucosaminidase / Q000032:analysis*; D010740:Phospholipases / Q000032:analysis*; D010741:Phospholipases A / Q000032:analysis*; D054467:Phospholipases A2
D001514:Bee Venoms; D006023:Glycoproteins; D010740:Phospholipases; D010741:Phospholipases A; D054467:Phospholipases A2; D000135:Acid Phosphatase; D006821:Hyaluronoglucosaminidase