A packing material for liquid chromatography, including particles of a copolymer having a monomer unit derived from a (meth)acrylic acid ester and a monomer unit derived from divinylbenzene, wherein a ratio between the monomer unit derived from a (meth)acrylic acid ester and the monomer unit derived from divinylbenzene is 70 mass % to 90 mass %:30 mass % to 10 mass %, wherein the particles each have a sulfo group bonded to a surface thereof and a structure in which the sulfo group is bonded includes a structure represented by the formula (1):

##STR00001##

where R X and n are as defined herein, and wherein the particles each include the sulfo group at from 40 mol/g to 300 mol/g. Also disclosed is a method of producing the packing material, a column packed with the packing material, and a method of analyzing glycated hemoglobin.

Novel compositions for removing impurities such as, protein aggregates, from a sample containing a protein of interest, e.g., an antibody. Such compositions can be used prior to the virus filtration step during protein purification, to remove aggregates and protect the virus filter from fouling, therefore improving virus filter capacity. A porous solid support including a co-polymer having at least two monomers, wherein at least one of the monomers comprises acrylamide and at least a second monomer comprises a hydrophobic binding group, where the solid support selectively binds protein aggregates, thereby to separate the monomeric protein of interest from the protein aggregates. The method can be performed under neutral to high pH and high conductivity conditions.

Novel compositions for removing impurities such as, protein aggregates, from a sample containing a protein of interest, e.g., an antibody. Such compositions can be used prior to the virus filtration step during protein purification, to remove aggregates and protect the virus filter from fouling, therefore improving virus filter capacity. A porous solid support including a co-polymer having at least two monomers, wherein at least one of the monomers comprises acrylamide and at least a second monomer comprises a hydrophobic binding group, where the solid support selectively binds protein aggregates, thereby to separate the monomeric protein of interest from the protein aggregates. The method can be performed under neutral to high pH and high conductivity conditions.

Provided are a protein L-derived immunoglobulin binding protein having an increased antibody dissociation rate under acidic conditions, and an affinity support using the same. Disclosed are an immunoglobulin binding protein comprising at least one mutant of an immunoglobulin binding domain, and an affinity support comprising a solid-phase support having the immunoglobulin binding protein bound thereto. A mutant of the immunoglobulin binding domain consists of an amino acid sequence having an identity of at least 85% with the sequence set forth in any one of SEQ ID NO:1 to SEQ ID NO:9 and a predetermined mutation, and the mutant has immunoglobulin chain binding activity.

Provided are a protein L-derived immunoglobulin binding protein having an increased antibody dissociation rate under acidic conditions, and an affinity support using the same. Disclosed are an immunoglobulin binding protein comprising at least one mutant of an immunoglobulin binding domain, and an affinity support comprising a solid-phase support having the immunoglobulin binding protein bound thereto. A mutant of the immunoglobulin binding domain consists of an amino acid sequence having an identity of at least 85% with the sequence set forth in any one of SEQ ID NO:1 to SEQ ID NO:9 and a predetermined mutation, and the mutant has immunoglobulin chain binding activity.

There is disclosed a relatively simple method to increase the performance of surface localised multi-valent affinity ligands whose target's isoelectric pH differs significantly from the ligand's optimal target-binding pH. This situation can result in ligand binding of target affecting local pH and subsequent binding of more target. Increasing the buffering capacity of the ligand via recombinant or other addition of charge groups to the ligand is expected to partially offset such effects, leading to enhanced binding capacity as well as possible secondary favourable alterations in regard to ligand elution pH, and non-specific surface binding of non-target proteins.

Disclosed herein are embodiments of matrixes made of a porous size exclusion support and a cationic moiety for separating one or more small molecules from one or more large molecules in a sample using differences in one or more properties such as the size of the molecules, charge of the molecules, the isoelectric point (pI) of the molecules, and/or any combination of these properties including methods, systems, and kit embodiments. Also disclosed herein are embodiments of a method of making the matrixes and using the matrixes for separating small molecules from one or more large molecules in a sample.

Disclosed herein are embodiments of matrixes made of a porous size exclusion support and a cationic moiety for separating one or more small molecules from one or more large molecules in a sample using differences in one or more properties such as the size of the molecules, charge of the molecules, the isoelectric point (pI) of the molecules, and/or any combination of these properties including methods, systems, and kit embodiments. Also disclosed herein are embodiments of a method of making the matrixes and using the matrixes for separating small molecules from one or more large molecules in a sample.

The invention discloses a functionalised chromatography medium, comprising: i) at least one non-woven layer (10) of polymeric nano fibres (20) comprising a plurality of nanofibre-nano fibre fusion points (30); ii) a grafted polymer coating covering the polymeric nanofibres and the nanofibre-nanofibre fusion points; iii) a plurality of ligand groups covalently bound to the grafted polymer coating, wherein the ligand groups are capable of interacting with a target biomolecule.

A chromatographic media for separating bio-polymers, the chromatographic media having cationic exchange properties and anionic exchange properties, the chromatographic media comprising: (a) non-porous substrate particles including an organic polymer, the substrate particles having a neutral hydrophilic layer at a surface of the non-porous substrate particles, in which the neutral hydrophilic layer is configured to reduce a binding of the bio-polymers directly to the non-porous substrate particles compared to a binding of the bio-polymer to the non-porous substrate particles without the neutral hydrophilic layer; (b) a charged first ion exchange layer bound to the substrate particles on top of the hydrophilic layer, the first ion exchange layer comprising first ion exchange groups; and (c) a charged second ion exchange layer bound to the substrate particles on top of the first ion exchange layer.