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Selected Publication:

SHR Neuro Cancer Cardio Lipid

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. [OPEN ACCESS]
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Authors Med Uni Graz:
Birner-Grünberger Ruth

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Plum Analytics:
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
peptide mapping
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