The major birch pollen allergen, Bet v 1, shows ribonuclease activity

✍ Scribed by Albrecht Bufe; Michael D. Spangfort; Helga Kahlert; Max Schlaak; Wolf-Meinhard Becker

• Book ID: 104658839
• Publisher: Springer-Verlag
• Year: 1996
• Tongue: English
• Weight: 574 KB
• Volume: 199
• Category: Article
• ISSN: 0032-0935
• DOI: 10.1007/bf00195733

✦ Synopsis

The major birch (Betula alba L.) pollen allergen, Bet v 1, has been shown to be homologous to pathogenesis-related proteins in a number of plants. Recently, it was demonstrated that a ginseng protein with high homology to an intracellular pathogenesis-related protein of parsley and to Bet v 1 is a ribonuclease (RNase). Birch pollen extract was separated in an RNase activity gel. Four major RNase bands were excised from the gel, reseparated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and identified by Western blotting with a specific Bet v 1 monoclonal antibody and patient's serum. Thus the monomer and the dimer of Bet v 1 showed RNase activity. Purified recombinant Bet v 1 was shown to degrade plant RNA. The RNase activity of recombinant Bet v 1 was 180 units.mg-1.