The present invention relates to a method for preparing a concentrate of polyvalent immunoglobulins with view to therapeutic use, from an initial solution of blood plasma or a plasma fraction enriched with immunoglobulins, comprising the steps for removing the protein contaminants by precipitation with caprylic acid in order to obtain a solution free of proteases, and for separating by chromatography on a fluidized bed the solution free of proteases, said method allowing a concentrate of human polyvalent immunoglobulins with a yield of more than 4.5 g of immunoglobulins per liter of blood plasma applied to be obtained.

The present invention relates to methods for purifying or enriching a biomolecule using multimodal resins and an elution buffer containing a Good's buffer.

The present disclosure provides purification platforms comprising a depth filter step and/or a hydrophobic interaction chromatography (HIC) step. Also disclosed herein are methods of using the purification platforms described herein and compositions obtained therefrom, such as pharmaceutical compositions.

A method for purifying a glycosylated recombinant protein of interest from a contaminant is disclosed that is suitable for industrial production purposes to remove galectins and other host cell contaminants, such as metallic cations, from recombinant therapeutic proteins.

The present invention is directed to a novel process for purifying a recombinant polypeptide from a solution comprising one or more impurities, wherein the process is a chromatography process which uses saccharin. The present invention also provides the use of saccharin in a process for purifying a recombinant polypeptide from a solution comprising one or more impurities, wherein the process is a chromatography process. The invention further provides a wash buffer for purifying using chromatography a recombinant polypeptide from a solution comprising one or more impurities, wherein the wash buffer comprises saccharin.

The subject invention pertains to proteins are purified by a mixed-mode chromatography system formed by attaching a ligand with cation exchange and hydrophobic 1,3-dioxoisoindolin-2-yl group functionalities to a large-pore support matrix, the only linkage between the ligand and the support matrix being a chain having a backbone of one, two, three, four, or five atoms between the hydrophobic group and the support matrix.

The invention discloses a separation matrix which comprises a plurality of separation ligands, defined by the formula R.sub.1-L.sub.1-N(R.sub.3)-L.sub.2-R, immobilized on a support, wherein R.sub.1 is a five- or six-membered, substituted or non-substituted ring structure or a hydroxyethyl or hydroxypropyl group; L.sub.1 is either a methylene group or a covalent bond; R.sub.2 is a five- or six-membered, substituted or non-substituted ring structure; L.sub.2 is either a methylene group or a covalent bond; R.sub.3 is a methyl group; and wherein if R.sub.1 is a hydroxyethyl group and L.sub.1 is a covalent bond, R.sub.2 is a substituted aromatic ring structure or a substituted or non-substituted aliphatic ring structure.

The present disclosure relates to a pharmaceutical highly efficient anti-TFPI antibody composition including an anti-TFPI antibody for treating hemophilia, in which the content of HCP in a drug substance is less than 10.0 ng/mg, and the content of LPA in the drug substance or the drug product is less than 1.0 ng/mg. According to the present disclosure, a highly efficient anti-TFPI antibody composition having very low contents of HCP and LPA may be provided by providing a separation/purification process capable of minimizing anti-TFPI antibody polymer generation, and may be effectively used for the treatment of antibody-induced hemophilia patients and for the prevention of blood coagulation disease.

The present invention relates to the use of redox agents for purification of the CRM 197 variant of diphtheria toxin. The invention further relates to multi-step purification of CRM 197 from bacterial fermentates.

Herein is reported a method for obtaining a polypeptide in monomeric form comprising the steps of a) providing a solution comprising the polypeptide in monomeric form and in aggregated form, wherein the ratio of monomeric to aggregated form is 4:1 or less as determined by size exclusion chromatography, b) performing a mixed-mode chromatography in bind-and-elute mode, or a hydrophobic interaction chromatography in flow-through mode, or a size-exclusion chromatography, and c) performing a weak cation exchange chromatography in bind-and-elute mode or flow-through mode, and thereby obtaining the polypeptide in monomeric form.