THE MAJOR BIRCH POLLEN ALLERGEN, BET-V-1, SHOWS RIBONUCLEASE-ACTIVITY

Citation
A. Bufe et al., THE MAJOR BIRCH POLLEN ALLERGEN, BET-V-1, SHOWS RIBONUCLEASE-ACTIVITY, Planta, 199(3), 1996, pp. 413-415
Citations number
10
Categorie Soggetti
Plant Sciences
Journal title
PlantaACNP
ISSN journal
00320935
Volume
199
Issue
3
Year of publication
1996
Pages
413 - 415
Database
ISI
SICI code
0032-0935(1996)199:3<413:TMBPAB>2.0.ZU;2-P
Abstract
The major birch (Betula alba L.) pollen allergen, Bet v 1, has been sh own to be homologous to pathogenesis-related proteins in a number of p lants. Recently, it was demonstrated that a ginseng protein with high homology to an intracellular pathogenesis-related protein of parsley a nd to Bet v 1 is a ribonuclease (RNase). Birch pollen extract was sepa rated in an RNase activity gel. Four major RNase bands were excised fr om the gel, reseparated by sodium dodecyl sulfate-polyacrylamide gel e lectrophoresis 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 w as shown to degrade plant RNA. The RNase activity of recombinant Bet v 1 was 180 units . mg(-1).