Abstract: The invention relates to a process for the selective concentration of immunoglobulins or other proteins that contain an Fc domain (target protein), comprising the following steps: a. preparing a solution that contains the target protein; b. incorporating an Fc-binding protein with precisely two binding sites under conditions that allow binding to occur; c. separating the precipitate from the liquid phase; d. undoing the binding of the target protein from the Fc-binding protein.

Abstract: The invention relates to a process for the selective concentration of immunoglobulins or other proteins that contain an Fc domain (target protein), comprising the following steps: a. preparing a solution that contains the target protein; b. incorporating an Fc-binding protein with precisely two binding sites under conditions that allow binding to occur; c. separating the precipitate from the liquid phase; d. undoing the binding of the target protein from the Fc-binding protein.

Abstract: The invention relates to a process for inactivating proteases by repeatedly changing the pH in the cell culture supernatant at the start of the process for the purification of biopharmaceuticals. The pH is adjusted first to 3-5, and then to 7-9.

Abstract: The present invention relates to methods of depleting impurities, in particular host cell proteins (HCP) and DNA from cell culture supernatants by means of protein A chromatography using a novel washing buffer.

Abstract: The invention relates to a process for the selective concentration of immunoglobulins or other proteins that contain an Fc domain (target protein), comprising the following steps: a. preparing a solution that contains the target protein; b. incorporating an Fc-binding protein with precisely two binding sites under conditions that allow binding to occur; c. separating the precipitate from the liquid phase; d. undoing the binding of the target protein from the Fc-binding protein.

Abstract: The present invention relates to methods of depleting impurities, in particular host cell proteins (HCP) and DNA from cell culture supernatants by means of protein A chromatography using a novel washing buffer.

Abstract: The invention relates to a method of finding suitable parameters for the chromatographic purification of biomolecules. The method consists of equilibration, charging, washing and eluting steps, this sequence of steps being carried out by the partial batch method. The parameters determined in small, preferably numerous parallel test batches provide conclusions as to the chromatography conditions under which a given biomolecule can be purified optimally by column chromatography, optionally even on a larger scale.

Abstract: The invention relates to a process for inactivating proteases by repeatedly changing the pH in the cell culture supernatant at the start of the process for the purification of biopharmaceuticals. The pH is adjusted first to 3-5, and then to 7-9.

Abstract: The invention relates to a process for the selective concentration of immunoglobulins or other proteins that contain an Fc domain (target protein), comprising the following steps: a. preparing a solution that contains the target protein; b. incorporating an Fc-binding protein with precisely two binding sites under conditions that allow binding to occur; c. separating the precipitate from the liquid phase; d. undoing the binding of the target protein from the Fc-binding protein.

Abstract: The invention relates to a method for optimizing the biophysical properties of molecules and derivatives of the Ig superfamily. The method is characterized in that as yet unrecognized helical structural elements with unknown structural, stability and folding roles have been identified as important determinants of correct and efficient structuring of antibody domains. The novel process for positively influencing the antibody properties and properties of other proteins that have the Ig folding pattern now consists of optimizing the properties of the short helical elements and in the transplantation of these elements between Ig domains.

Abstract: The invention relates to methods of increasing the titre of a protein of interest in a cell as well as the improved production and purification of optimised biomolecules, one component of which is the domain CH3. A frequently observed effect in biomolecules is the cleaving of the C-terminal amino acid(s), e.g. the C-terminal lysine. The usually incomplete processing of the heavy chain of antibodies for example leads to product heterogeneity. To prevent this product heterogeneity the corresponding codon of the C-terminal lysine of the heavy antibody chain has been deleted by recombinant DNA technology. These optimised antibodies lead to a product titre which is higher than in the wild-type. In addition, they prove advantageous during purification by having better elution characteristics as a result of the reduced charge heterogeneity.

Abstract: The present application discloses a solid support material having covalently immobilized thereon an affinity ligand, said ligand comprising one or more hydrophobic functional group(s) and one or more cationic functional group(s) or one or more heteroaromatic functional group(s), wherein at least one hydrophobic functional group is separated from at least one cationic/heteroaromatic functional group by a through bond distance of from 5 ? to 20 ?, wherein said ligand has a molecular weight of from 120 Da to 5,000 Da. Typically, the affinity resin has a binding capacity larger than 5 mg monoclonal antibody per mL of affinity resin. A method for the isolation of biomolecules, such as proteins, in particular antibodies, such as monoclonal antibodies, or derivatives thereof, is also disclosed.

Abstract: A method of preparing a biotinylated polypeptide in a cell-free peptide synthesis reaction mixture by contacting, under suitable conditions, a polypeptide to be biotinylated, with a reaction mixture that includes ribosomes, tRNA, ATP, GTP, nucleotides, biotin and amino acids, and a polypeptide that includes an enzymatically active domain of a BirA enzyme. The polypeptide to be biotinylated includes a BirA substrate sequence tag, and the polypeptide to be biotinylated and the polypeptide comprising an enzymatically active domain of a BirA enzyme, are expressed in situ in the reaction mixture, by at least one nucleic acid molecule encoding the polypeptide to be biotinylated, and the enzymatically active domain of a BirA enzyme, respectively.

Abstract: The invention relates to a method of finding suitable parameters for the chromatographic purification of biomolecules. The method consists of equilibration, charging, washing and eluting steps, this sequence of steps being carried out by the partial batch method. The parameters determined in small, preferably numerous parallel test batches provide conclusions as to the chromatography conditions under which a given biomolecule can be purified optimally by column chromatography, optionally even on a larger scale.

Abstract: A method of preparing a biotinylated polypeptide in a cell-free peptide synthesis reaction mixture by contacting, under suitable conditions, a polypeptide to be biotinylated, with a reaction mixture that includes ribosomes, tRNA, ATP, GTP, nucleotides, biotin and amino acids, and a polypeptide that includes an enzymatically active domain of a BirA enzyme. The polypeptide to be biotinylated includes a BirA substrate sequence tag, and the polypeptide to be biotinylated and the polypeptide comprising an enzymatically active domain of a BirA enzyme, are expressed in situ in the reaction mixture, by at least one nucleic acid molecule encoding the polypeptide to be biotinylated, and the enzymatically active domain of a BirA enzyme, respectively.

Abstract: A polypeptide with the properties of collagenase class I from Clostridium histolyticum (CHC I) and the amino acid sequence SEQ ID NO:2 which is optionally N-terminally extended by one or several amino acids of the sequence SEQ ID NO:3 is advantageously suitable for the isolation of cells from mammalian tissue and human tissue.

Abstract: A process for the production of a naturally folded eukaryotic polypeptide containing two or several cysteines linked by disulfide bridges by a) culturing prokaryotic cells in which the said prokaryotic cells contain an expression vector which codes for the said polypeptide which contains a prokaryotic signal sequence at the N-terminus, b) secreting the polypeptide into the periplasm or the medium, c) cleaving the signal sequence and isolating the polypeptide from the periplasm or the medium, which is characterized in that a nucleic acid coding for a molecular chaperone is additionally expressed in the said prokaryotic cell and the chaperone is secreted into the periplasm, is suitable for the recombinant production of polypeptides in prokaryotes in a high yield.

Abstract: A nucleic acid, which can be used to express a polypeptide with interleukin-16 activity in a prokaryotic or eukaryotic host cell, wherein the said nucleic acid codes for a polypeptide with the amino acid sequence SEQ ID NO:2 and/or a SEQ ID NO:2 N-terminally elongated by Ala-Ser or a form thereof which is shortened at its C-terminus by up to 8 amino acids, is suitable for producing an active IL-16 polypeptide.

Abstract: A process produces a water-soluble, naturally folded eukaryotic polypeptide containing two or several cysteines linked by disulfide bridges. This process involves culturing prokaryotic cells, a) in which the prokaryotic cells contain an expression vector which encodes the polypeptide which contains a prokaryotic signal sequence at the N-terminus, b) under conditions under which the polypeptide is secreted into the periplasm or the medium, c) cleaving the signal sequence and isolating the polypeptide from the periplasm or the medium. In this process, the culturing is carried out in the presence of arginine or a compound of the formula I R2—CO—NR1 (I) in which R and R1 represent hydrogen or a saturated or unsaturated branched or unbranched C1-C4 alkyl chain and R2 represents hydrogen, NHR1 or a saturated or unsaturated branched or unbranched C1-C3 alkyl chain, is suitable for the recombinant production of polypeptides in prokaryotes in a high yield.

Abstract: Oxygen-independent cholesterol-converting enzyme obtainable from Actinomycetes or Basidiomycetes which utilizes artificial electron acceptors as well as a method and reagent for the determination of (total) cholesterol using the enzyme.