Abstract: A process is provided for inhibiting symptoms of celiac disease, Clostridium difficile associated diseases such as Clostridium difficile colitis, pseudomembranous colitis and antibiotic associated diarrhea, food allergy or food intolerance in a subject that includes the oral administration to the subject suffering from food allergy or food intolerance an IgM. When administered in a, therapeutic quantity based on the subject characteristics and the type of IgM, symptoms of food allergy or food intolerance in that subject are inhibited. Even non-secretory forms of IgM are effective when administered orally.

Abstract: Disclosed here includes a method for purifying a biologic composition, comprising diafiltering the biologic composition into a composition comprising phosphate buffered saline (PBS) to obtain a purified composition. The method disclosed here can be particularly useful for removing one or more impurities from the biologic composition, such as bis(2-hydroxyethyl)amino-tris(hydroxymethyl)methane (Bis-tris).

Abstract: The invention provides methods of reducing fouling of ultrafiltration membranes in processes wherein virus particles are removed from aqueous solutions comprising virus particles and at least one protein by adding a surfactant or non-surfactant, non-ionic agent to the aqueous solution prior to filtration. The invention also provides methods to dissociate protein aggregates or to reduce the formation of protein aggregates by adding a surfactant or non-surfactant, non-ionic agent to the protein solution.

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: Provided is an affinity chromatography carrier having an excellent purification purity, including a substrate, a hydrophilic polymer, and an affinity ligand, in which the substrate is constituted of at least one selected from the group consisting of a polysaccharide, an acrylate-based polymer, a methacrylate-based polymer and a styrene-based polymer, the hydrophilic polymer is at least one selected from the group consisting of hydrophilic polysaccharides, the affinity ligand is at least one selected from the group consisting of an antibody-binding protein and an antibody-binding polypeptide, a carboxy group is introduced into the affinity chromatography carrier, and the amount of the carboxy group introduced is 15 mmol/L-gel to 60 mmol/L-gel in terms of ion exchange capacity.

Abstract: The present invention relates to improved processes and systems for purification of biological molecules, where the processes can be performed in a continuous manner.

Abstract: A composition containing an antibody is prepared in such a state that the composition contains an anionic polymer at pH lower than the pI of the antibody, and impurities insolubilized by the anionic polymer are removed. More preferably, the composition is prepared in such a state that the composition contains an anionic polymer at pH lower than or equal to the pI of the antibody minus one, and impurities insolubilized by the anionic polymer are removed.

Abstract: An affinity separation matrix includes a water-insoluble base material; and a ligand that is immobilized on the water-insoluble base material, wherein the ligand is an antibody ? chain variable region-binding peptide comprising B5 domain of Protein L derived from Peptostreptococcus magnus 312 strain or a part thereof.

Abstract: A method for purifying an antibody or an antibody fragment containing ?-chain variable region includes adsorbing at least one of the antibody or the antibody fragment onto an affinity separation matrix by contacting a liquid sample with the affinity separation matrix, washing the affinity separation matrix to remove impurities, and separating the at least one of the antibody or the antibody fragment from the affinity separation matrix by using an acetate buffer. The liquid sample includes the at least one of the antibody or the antibody fragment. The affinity separation matrix includes a water-insoluble carrier and a ligand selected from the group consisting of Protein L, a variant of Protein L, a domain of Protein L, and a variant of the domain. The ligand is immobilized on the water-insoluble carrier.

Abstract: The present disclosure relates to non-natural binding proteins comprising one or more non-natural immunoglobulin (Ig) binding domains wherein at least one non-natural lg-binding domain comprises the amino acid sequence X1 X2X3XiXsX5X7 XsQQX11AFYX1sX15LX1 sX19PX21 LX23X24X2sQRX28X2gf IQSLKDDPSXio SXi2Xi3Xi4LXi5EAXigKLXs2Xs3Xs4QXs5PX. The disclosure also relates to compositions such as affinity matrices comprising the non-natural Ig-binding proteins of the invention. Use of these Ig-binding proteins or of the compositions for affinity purification of immunoglobulins and to methods of affinity purification.

Abstract: A first immunoglobulin ? chain variable region-binding peptide includes an amino acid sequence of SEQ ID NO: 21 with substitution of one or more amino acid residues at the 15th position, the 16th position, the 17th position or the 18th position, wherein an acid dissociation pH thereof is shifted to a neutral side. A second immunoglobulin ? chain variable region-binding peptide further includes deletion, substitution and/or addition of 1-20 amino acid residues at positions other than the 15th position, the 16th position, the 17th position and the 18th position. A third immunoglobulin ? chain variable region-binding peptide includes an amino acid sequence with a sequence identity of 80% or more to the amino acid sequence of the first immunoglobulin ? chain variable region-binding peptide.

Abstract: The present invention relates to the purification of target molecules like recombinant and/or biotherapeutic proteins. Activated carbon can be used to remove leachables and/or extractables resulting from disposable equipment employed in the process.

Abstract: The invention provides a three-step chromatography process for small and large-scale purification of proteins, specifically monoclonal antibodies, using only four buffer solutions made from a mother solution.

Abstract: Methods for purifying multispecific antibodies on interest (MAIs) that co-engage at least two different antigens or epitopes (also referred to targets, used interchangeably throughout), from compositions comprising the MAI and parental homodimeric antibody species are provided, as well as reagents which may be used to practice such methods.

Abstract: To provide an affinity support in which a binding property of a ligand to a target substance is improved. The affinity support contains a solid phase support and a protein ligand, wherein the protein ligand is represented by formula (1): R—R1 (1) wherein R represents a linker binding to the solid phase support, which contains a polyproline, and R1 represents a protein showing an affinity to immunoglobulin, and the R is bound to a C terminal or an N terminal of an amino acid sequence in R1.

Abstract: The present invention provides, among other aspects, methods for the manufacture of plasma-derived immunoglobulin G compositions highly enriched for anti-brain disease related protein antibodies (e.g., anti-A?, anti-RAGE, and anti-?-synuclein antibodies). Advantageously, the methods provided do not affect the manufacturing processes or capabilities for producing plasma-derived IgG therapeutics. Plasma-derived IgG compositions that are highly enriched for anti-brain disease related protein antibodies (e.g., anti-A?, anti-RAGE, and anti-?-synuclein antibodies), as also provided here. Methods for the treatment of brain diseases and disorders by administration of plasma-derived IgG compositions highly enriched for anti-brain disease related protein antibodies (e.g., anti-A?, anti-RAGE, and anti-?-synuclein antibodies), are also provided.

Abstract: In certain embodiments, the invention provides a method of purifying a protein of interest from a mixture which comprises the protein of interest and one or more contaminants, comprising: a) subjecting the mixture to a first chromatography step; b) recovering the protein of interest in an elution solution; c) adding caprylic acid to the elution solution to form a contaminant precipitate; d) removing the contaminant precipitate from the elution solution; and e) subjecting the post-precipitated elution solution to a second chromatography column, thereby purifying the protein of interest.

Abstract: For the removal of high molecular weight compounds from recombinantly produced polypeptides generally chromatographic methods are employed. It has been found that underivatized controlled pore glass (uCPG) selectively binds high molecular weight compounds present in a solution. The purified polypeptide can be recovered e.g. from the flow through of a chromatography column containing uCPG as chromatography material. It has been found that this effect is pronounced at a pH value of about 4 to 6 in buffered solutions. With approximately 100 m2 to 150 m2 uCPG surface per g of polypeptide almost 80% to 95% of the high molecular weight compounds are removed with a yield of 80% to 90% of polypeptide.

Abstract: Provided is an affinity chromatography carrier that maintains high immunoglobulin-binding capacity and high alkali resistance. An immunoglobulin-binding protein including at least one modified immunoglobulin-binding domain, the modified immunoglobulin-binding domain being a polypeptide consisting of an amino acid sequence of an immunoglobulin-binding domain selected from the group consisting of the B domain, Z domain, C domain, and variants thereof of Staphylococcus aureus protein A, in which at least one amino acid residue is inserted between positions corresponding to the 3-position and position 4 of the amino acid sequence of the B domain, Z domain or C domain.

Abstract: Eculizumab, a humanized monoclonal antibody against C5 that inhibits terminal complement activation, showed activity in a preliminary 12-week open-label trial in a small cohort of patients with paroxysmal nocturnal hemoglobinuria (PNH). The present study examined whether chronic eculizumab therapy could reduce intravascular hemolysis, stabilize hemoglobin levels, reduce transfusion requirements, and improve quality of life in a double-blind, randomized, placebo-controlled, multi-center global Phase III trial. It has been found that eculizumab stabilized hemoglobin levels, decreased the need for transfusions, and improved quality of life in PNH patients via reduced intravascular hemolysis. Chronic eculizumab treatment appears to be a safe and effective therapy for PNH.