Medizinische Universität Graz Austria/Österreich - Forschungsportal - Medical University of Graz
Gewählte Publikation:
SHR Neuro Krebs Kardio Lipid Stoffw Microb
Suck, R; Kamionka, T; Schäffer, B; Wahl, R; Nandy, A; Weber, B; Petersen, A; Birner-Grünberger, R; D V, SC; Keller, W; Fiebig, H; Cromwell, O.
Bacterially expressed and optimized recombinant Phl p 1 is immunobiochemically equivalent to natural Phl p 1.
Biochim Biophys Acta. 2006; 1764(11): 1701-1709.
Doi: 10.1016/j.bbapap.2006.09.015
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- Co-Autor*innen der Med Uni Graz
- Birner-Grünberger Ruth
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- Abstract:
- Recombinant production in bacteria of soluble and monomeric Phl p 1, a major allergen of Timothy grass pollen, has proved to be very problematic. In order to facilitate expression and purification of this allergen, a recombinant variant was designed with a single amino acid substitution. Several comparative analyses with natural counterparts using electrophoretic and HPLC separations, together with immunological assays, demonstrated high equivalence. This is the first description of an approach aiming at an improvement of a natural like recombinant allergen.
- Find related publications in this database (using NLM MeSH Indexing)
- Allergens - chemistry
- Amino Acid Sequence - chemistry
- Chromatography, High Pressure Liquid - chemistry
- Circular Dichroism - chemistry
- Electrophoresis, Polyacrylamide Gel - chemistry
- Immunohistochemistry - chemistry
- Molecular Sequence Data - chemistry
- Molecular Weight - chemistry
- Peptide Mapping - chemistry
- Plant Proteins - chemistry
- Recombinant Proteins - genetics
- Sequence Homology, Amino Acid - genetics
- Find related publications in this database (Keywords)
- rPhl p 1 variant
- Dac g 1
- Lol p 1
- bacterial expression
- IgE-binding
- peptide mapping