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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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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
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Electrophoresis, Polyacrylamide Gel - chemistry
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Molecular Sequence Data - chemistry
Molecular Weight - chemistry
Peptide Mapping - chemistry
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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
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