Sandoz Ag

Boehringer Ingelheim Rcv Gmbh & Co. Kg

Bia Separations D.o.o.

Rainer Hahn

Alois A Jungbauer

Waltraud Kaar

Alexandru Trefilov

Anne Tscheliessnig

Ales Strancar

Clemens Achmüller

Bernhard Auer

Philipp Wechner

Milos Barut

Ales Podgornik

Moritz Imendoerffer

Michael Seifert

Alois Jungbauer

The present invention provides novel methods of cell disruption and release of biomolecules from a cell. The invention comprises the use of positively and/or negatively charged microparticles comprising ground resin. It is particularly useful for purification of biomolecules from cell culture.

Microparticles for cell disruption and/or biomolecule recovery

The present invention provides a novel adsorbent composition for recovering biomolecules from a fluid. The composition comprises positively and negatively charged microparticles in the form of ground particles. The adsorbent is particularly useful for purification of biomolecules from the cell culture.

Adsorbent composition and use thereof

Disclosed is a method for the production of a heterologous polypeptide of interest with a homogenous N-terminus, using a fusion polypeptide comprising the polypeptide of interest and N-terminally thereto a polypeptide exhibiting autoproteolytic function, said method comprises the steps of a) binding of the fusion polypeptide in a soluble, autoproteolytically inactive form by an affinity chromatography system, b) refolding of the fusion polypeptide, thereby activating the autoproteolytic function of the fusion polypeptide and causing cleavage of the heterologous polypeptide of interest, and c) subsequently eluting the heterologous polypeptide of interest, wherein the steps are conducted on one affinity chromatography system.

Production of recombinant proteins by autoproteolytic cleavage of a fusion protein

Disclosed is a method for the production of a heterologous polypeptide of interest with a homogenous N-terminus, using a fusion polypeptide comprising the polypeptide of interest and N-terminally thereto a polypeptide exhibiting autoproteolytic function, said method comprising the steps of a) binding of the fusion polypeptide in a soluble, autoproteolytically inactive form by an affinity chromatography system, b) refolding of the fusion polypeptide, thereby activating the autoproteolytic function of the fusion polypeptide and causing cleavage of the heterologous polypeptide of interest, and c) subsequently eluting the heterologous polypeptide of interest, wherein said steps are conducted on one affinity chromatography system.

Disclosed is an affinity matrix comprising a solid phase and an affinity ligand comprising peptide bonds coupled to this solid phase, wherein the affinity ligand comprising peptide bond is selected from the following group of ligands: a) peptides comprising the formula XXXX, wherein Xto Xare amino acid residues and at least two of Xto Xis W, Y or F; b) peptides comprising the formula XXXX, wherein Xto Xare amino acid residues, at least one of Xto Xis W, and at least one of Xto Xis E or D; and c) poly-amino acids consisting of an amino acid monomer of the group consisting of R, K, E and D and an amino acid monomer of the group consisting of Y, F and W, preferably poly-KY, poly-KF, poly-KW, poly-RY, poly-RF, poly-RW, poly-EY, poly-DY, poly-EF, poly-EW, poly-DF and poly-DW, with the proviso that the peptides according to a) and b) have a maximum length of 35 amino acid residues and that the poly-amino acids according to c) have a minimum length of 20 amino acid residues.

Affinity ligands

Chromatography material and a process of manufacturing that material

Growing community of inventors

Vienna, Austria

Rainer Hahn