Medizinische Universität Graz Austria/Österreich - Forschungsportal - Medical University of Graz

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Gewählte Publikation:

Schnütgen, F; Börchers, T; Müller, T; Spener, F.
Heterologous expression and characterisation of mouse brain fatty acid binding protein.
Biol Chem Hoppe Seyler. 1996; 377(3):211-215
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Autor/innen der Med Uni Graz:
Spener Friedrich
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Abstract:
A novel brain-type member of the fatty acid binding protein family (B-FABP) was heterologously expressed in Escherichia coli, either as inclusion bodies at 37 degrees C or in soluble form at 22 degrees C. Both B-FABP renatured from inclusion bodies and the solubly expressed protein could be purified to homogeneity by anion exchange chromatography and gel filtration in a functional conformation as they bound oleic acid with high affinity. None of the five cysteines of B-FABP was involved in disulphide bond formation. Isoelectric focusing revealed heterogeneity of the renatured protein but not of the solubly expressed protein. By Western blotting using affinity purified rabbit antibodies raised against the recombinant B-FABP it was demonstrated that in adult mice, B-FABP is predominantly expressed in the olfactory bulb.
Find related publications in this database (using NLM MeSH Indexing)
Amino Acid Sequence -
Animals -
Brain - metabolism
Carrier Proteins - genetics Carrier Proteins - isolation and purification Carrier Proteins - metabolism
Cloning, Molecular -
Escherichia coli -
Fatty Acid-Binding Proteins -
Isoelectric Point -
Mice -
Molecular Sequence Data -
Myelin P2 Protein - genetics Myelin P2 Protein - isolation and purification Myelin P2 Protein - metabolism
Neoplasm Proteins -
Nerve Tissue Proteins -
Oleic Acid -
Oleic Acids - metabolism
Rabbits -
Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - isolation and purification Recombinant Fusion Proteins - metabolism

Find related publications in this database (Keywords)
fatty acid binding
inclusion bodies
pET expression vector
recombinant protein
renaturation
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