Characterisation of recombinant isoforms of birch pollen allergen Bet v 1
(1996) In Advances in Experimental Medicine and Biology 409. p.251-254- Abstract
- Three isoforms of the major birch pollen allergen, Bet v, 1 from Betula verrucosa have been expressed as recombinant proteins in E. coli and purified. The immunochemical properties of recombinant isoforms (rBet v 1) differed on immunoblots when compared using Mabs and birch pollen allergic patients serum IgE. 2-D gel analysis showed that recombinant isoforms with different epitope structure can focus under the same protein spot after electrophoresis. The structure of conformational epitopes can be distorted by amino acid substitutions even when T-cell epitopes are not affected as judged by T-cell proliferation studies.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1110040
- author
- Spangfort, M D ; Ipsen, H ; Sparholt, S H ; Aasmul-Olsen, S ; Osmark, Peter LU ; Poulsen, F M ; Larsen, M ; Mortz, E ; Roepstorff, P and Larsen, J N
- organization
- publishing date
- 1996
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Advances in Experimental Medicine and Biology
- volume
- 409
- pages
- 251 - 254
- publisher
- Springer
- external identifiers
-
- pmid:9095250
- scopus:8244227328
- ISSN
- 0065-2598
- language
- English
- LU publication?
- yes
- id
- 767a1cda-e1d4-479e-ba2e-76148c470197 (old id 1110040)
- date added to LUP
- 2016-04-01 15:59:59
- date last changed
- 2025-04-04 14:11:53
@article{767a1cda-e1d4-479e-ba2e-76148c470197, abstract = {{Three isoforms of the major birch pollen allergen, Bet v, 1 from Betula verrucosa have been expressed as recombinant proteins in E. coli and purified. The immunochemical properties of recombinant isoforms (rBet v 1) differed on immunoblots when compared using Mabs and birch pollen allergic patients serum IgE. 2-D gel analysis showed that recombinant isoforms with different epitope structure can focus under the same protein spot after electrophoresis. The structure of conformational epitopes can be distorted by amino acid substitutions even when T-cell epitopes are not affected as judged by T-cell proliferation studies.}}, author = {{Spangfort, M D and Ipsen, H and Sparholt, S H and Aasmul-Olsen, S and Osmark, Peter and Poulsen, F M and Larsen, M and Mortz, E and Roepstorff, P and Larsen, J N}}, issn = {{0065-2598}}, language = {{eng}}, pages = {{251--254}}, publisher = {{Springer}}, series = {{Advances in Experimental Medicine and Biology}}, title = {{Characterisation of recombinant isoforms of birch pollen allergen Bet v 1}}, volume = {{409}}, year = {{1996}}, }