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.

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 present invention provides the use of charged surface reversed phase chromatographic materials along with standard reversed-phase LC and mass spectrometry compatible conditions for the retention, separation, purification, and characterization of acidic, polar molecules, including, but not limited to, organic acids, α-amino acids, phosphate sugars, nucleotides, other acidic, polar biologically relevant molecules. The chromatographic materials of the invention are high purity chromatographic materials comprising a chromatographic surface wherein the chromatographic surface comprises a hydrophobic surface group and one or more ionizable modifier.

Systems and methods that facilitate the automatic (or substantially automatic) preparation of a sample of a product containing molecules for analysis and automatic (or substantially automatic) performance of an assay of that sample. Thus, the preparation and analysis can be performed substantially in-real time, or, in other words, much more quickly than presently allowed by conventional systems and methods.

The present disclosure provides purification platforms comprising a depth filter step and/or a hydrophobic interaction chromatography (HIC) step and/or a MM-HIC/IEX chromatography step, and are useful for providing a method of reducing a hydrolytic enzyme activity rate of a composition obtained from said purification platforms. Also disclosed herein are methods of using the purification platforms described herein and compositions obtained therefrom, such as pharmaceutical compositions.

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.

A chromatography analysis apparatus (30) comprises: a fractionation device (32) for receiving a sample, the fractionation device (32) defining a sample flow path that includes a guard column; and a fractionation output analyser (34), wherein a fractionation output of the guard column is provided to an input of the fractionation output analyser (34) for enabling subsequent analysis of the fractionation output by the fractionation output analyser (34).

Provided are a medium composition for culturing animal cells for producing a recombinant extracellular matrix protein, a method of producing the recombinant extracellular matrix protein with high purity, and a method of assaying a monomer of the recombinant extracellular matrix protein.

Problems to be Solved

The present invention provides an affinity support capable of trapping a substance by cooperative binding that is less likely to cause dissociation even when the substance is a molecule other than an antibody, and a trapping method using the same.

Means to Solve the Problems

A method of trapping a substance comprising the step of contacting an objective to be trapped with an affinity support comprising a support, a spacer bound to the support and an affinity substance bound to the spacer, so as to bind the objective to be trapped to the affinity substance, wherein each one of the objective to be trapped has a plural of affinity sites and the affinity substance binds to at least two of the affinity sites simultaneously.

A cyclic chromatographic purification method for the isolation of a product from a feed mixture consisting of the product and at least one further component representing impurities, which impurities bind stronger to the chromatographic stationary phase than the product is given. The method uses at least two chromatographic adsorbers as chromatographic stationary phase, grouped into only one first adsorber section (1) and one second adsorber section (2), wherein if an adsorber section comprises more than one chromatographic adsorber these are permanently connected in series, wherein the first adsorber section (1) has a first adsorber section inlet and a first adsorber section outlet, and the second adsorber section (1) has a second adsorber section inlet and a second adsorber section outlet.