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   <subfield code="a">The major birch pollen allergen, Bet v 1, shows ribonuclease activity</subfield>
   <subfield code="h">[Elektronische Daten]</subfield>
   <subfield code="c">[Albrecht Bufe, Michael Spangfort, Helga Kahlert, Max Schlaak, Wolf-Meinhard Becker]</subfield>
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   <subfield code="a">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.</subfield>
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