The invention relates to a method for extracting mycotoxins from grain and other food products or from feed and its subsequent quantification. Fields of application are the food industry, the animal feed industry or biotechnology. The objective of the present invention is to develop an extraction method with which it is possible to uniformly extract mycotoxins with different dissolving properties. It was found that with the aid of aqueous, buffered naphthyl and/or phenyl compounds or their heterocyclical analogues, both hydrophobic and hydrophilic mycotoxins can be extracted. The method according to the invention is characterized in that the buffered solutions of naphthyl and/or phenyl compounds and/or their heterocyclical analogues, which carry at least one sulphonic acid or at least one carbonate acid group, are brought into contact with the grain or other food products or animal feed, the aqueous solution is then separated and the content of the extracted mycotoxins in the aqueous solution is determined.

Method and apparatuses for forming gel droplets including biological tissue (e.g., cells), and in particular, methods and apparatuses for removing oil from the gel droplets comprising dissociated cells (including micro-organospheres) are described herein. Although it is beneficial to use oil in the formation of these gel droplets, and particularly micro-organospheres, oil may inhibit growth and survival of the cells within the gel droplets. The methods and apparatuses described herein may permit the removal of oil and may enhance survival and quality of the resulting gel droplets.

Method and apparatuses for forming gel droplets including biological tissue (e.g., cells), and in particular, methods and apparatuses for removing oil from the gel droplets comprising dissociated cells (including micro-organospheres) are described herein. Although it is beneficial to use oil in the formation of these gel droplets, and particularly micro-organospheres, oil may inhibit growth and survival of the cells within the gel droplets. The methods and apparatuses described herein may permit the removal of oil and may enhance survival and quality of the resulting gel droplets.

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.

An object of the present invention is to provide a material which can remove an activated leukocyte-activated platelet complex with high efficiency. The present invention provides a material for removing an activated leukocyte-activated platelet complex, the material being a water-insoluble carrier to the surface of which carrier a compound(s) having a charged functional group(s) is(are) bound, wherein an extending length ratio of the surface is 4 to 7.

The present invention relates to a novel polypeptide affinity ligand coupled to solid supports and affinity purification of IgG antibodies. The invention is comprised of (1) the design, generation, and purification of polypeptide ligands, (2) coupling of a polypeptide affinity ligand to a solid support matrix, (3) purification of IgG (polyclonal and monoclonal antibodies), and (4) cleaning and reuse of polypeptide supported solid matrix.

A process for synthesizing and separating secretory IgA from a mixture of IgA monmer and IgA dimer is provided. The process includes covalently binding affinity tagged or epitope tagged recombinant secretory component to the IgA dimer in the mixture and binding the affinity tagged or an epitope tagged secretory IgA to immobilized moieties on the solid phase support resin to which the affinity tag or epitope tag binds and then eluting the affinity tagged or an epitope tagged secretory IgA with release buffer. A process for synthesizing and separating secretory IgM from a mixture of IgM and other plasma proteins is also provided. The process includes covalently binding affinity tagged or an epitope tagged recombinant secretory component to the IgM in the mixture and binding the affinity tagged or an epitope tagged secretory IgM to immobilized moieties on the solid phase support resin and then eluting the peptide tagged secretory IgM with a release buffer.

The invention provides methods for quantifying a non-ionic surfactant in a composition comprising a polypeptide and the non-ionic surfactant, where the quantification exhibits reduced interference between the non-ionic surfactant and the polypeptide. Also provided are methods where the composition further includes N-acetyl tryptophan, and the quantification exhibits reduced interference between the non-ionic surfactant, the polypeptide, and N-acetyl tryptophan.

Provided herein are methods of preparing EVs, e.g., exosomes, associated with or encapsulated various cyclic dinucleotides, including STING agonists. Also provided herein are methods of loading EVs, e.g., exosomes, with various cyclic dinucleotides, including STING agonists.

The invention relates to a Protein A chromatography step of a purification process for a therapeutic protein, wherein a load solution including the therapeutic protein is applied onto a Protein A chromatography medium. According to the invention, a solution comprising CaCl.sub.2 is used as a wash solution for the Protein A chromatography medium for enhancing the removal of lipases, in particular phospholipase B-like 2 (PLBL2). The invention is of particular interest for the purification of CHO-expressed antibodies, such as tanezumab.