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

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 r...

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Bibliographic Details
Published in:Planta 1996, Vol.199 (3), p.413-415
Main Authors: Bufe, A, Spangfort, M.D, Kahlert, H, Schlaak, M, Becker, W.-M. (Research Center Borstel (Germany). Molecular Allergology)
Format: Article
Language:English
Subjects:
ACTIVIDAD ENZIMATICA
ACTIVITE ENZYMATIQUE
ALERGENOS
ALLERGENE
ALLERGENS
Allergens - isolation & purification
Allergens - metabolism
Allergies
Amino Acid Sequence
Antigens, allergens
Antigens, Plant
Baumschule
Betting
BETULA ALBA
Biological and medical sciences
Biotechnology
Birkenpollenallergen
ENZYMIC ACTIVITY
Fundamental and applied biological sciences. Psychology
Fundamental immunology
Gels
Immediate hypersensitivity. Allergy. Anaphylaxis, etc
Immunobiology
IMMUNOLOGICAL TECHNIQUES
India ink
Molecular Sequence Data
Monoclonal antibodies
PANAX PSEUDOGINSENG
Parsley
PATHOGENESE
PATHOGENESIS
PATOGENESIS
Pflanzenphysiologie
Plant Proteins - isolation & purification
Plant Proteins - metabolism
POLEN
POLLEN
Pollen - metabolism
PROTEINAS
PROTEINE
PROTEINS
RIBONUCLEASAS
RIBONUCLEASE
RIBONUCLEASES
Ribonucleases - isolation & purification
Ribonucleases - metabolism
RNA
Sequence Homology, Amino Acid
TECHNIQUE IMMUNOLOGIQUE
TECNICAS INMUNOLOGICAS
Trees
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Description
Summary: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.
ISSN:0032-0935
1432-2048
DOI:10.1007/bf00195733