The invention provides a sorbent material comprising a PSA that is synthesized via a sol-gel process. The sorbent material enables higher loading of PSA and other functional groups than conventional sorbents. The sorbent material can further encapsulate carbonaceous and/or non-carbonaceous particles that are distributed throughout the sorbent network. The invention also relates to a method of making the sorbent materials.

A chromatography device for removing a solute from a fluid is provided. The device has a first plate having an inlet and a first channel. The first channel directs the fluid from the inlet towards chromatographic media housed in a chamber coupled to the first plate. The chamber has a leading edge for receiving the fluid from the first channel and a trailing edge for delivering the fluid to a second channel. The chromatographic media is configured to remove the solute from the fluid as the fluid passes through the chamber. The device also has a second plate coupled to the chamber having the second channel and an outlet. The second channel directs the fluid from the chamber to the outlet. The direction of flow of fluid through the first channel and the second channel is transverse to a direction of flow of the fluid through the chromatographic media. A method of removing a solute from a fluid is also provided.

The present invention provides novel chromatographic materials, e.g., for chromatographic separations, processes for its preparation and separations devices containing the chromatographic material; separations devices, chromatographic columns and kits comprising the same; and methods for the preparation thereof. The chromatographic materials of the invention are superficially porous chromatographic particulate materials comprising sized less than 2 microns.

Methods are provided for making rapid labeled dextran ladders and other calibrants useful in liquid chromatography. The methodologies include a two-step process comprising a reductive amination step of providing a reducing glycan and reacting it with a compound having a primary amine to produce an intermediate compound. The intermediate compound is then rapidly tagged with a rapid tagging reagent to produce the rapid labeled dextran ladder.

The object of the invention relates to an extraction cell (100) used in a centrifugal partition chromatograph, which has a cell wall (120) determining a closed extraction chamber (150), as well as an inlet (115) and an outlet (140) ensuring the fluid connection between the extraction chamber (150) and the space outside of the extraction cell (100) formed on essentially opposite parts of the cell wall (120).

The extraction cell (100) according to the invention is constructed asymmetrically from the point of view of the reversibility of the direction of flow used when the centrifugal partition chromatograph is in operation.

A sol-gel sorbent or chromatography stationary phase is a particulate metal oxide gel containing polymeric segments uniformly distributed throughout the metal oxide gel. The metal oxide gel is an oxide from silicone or other metal oxide that can have one of the valence bonds attached to an organic group and the remainder occupied by oxygens that can be provided as an oxide or an alkoxide or aryl oxide of the polymeric segments. The particles are used for an SPE sorbent or as a packing for a reversed phase high-performance liquid chromatography (RP-HPLC), a normal phase high-performance liquid chromatography (NP-HPLC) column or a hydrophilic interaction liquid chromatography (HILIC) column.

The invention relates to poly-amide bonded hydrophilic interaction chromatography (HILIC) stationary phases and novel HILIC methods for use in the characterization of large biological molecules modified with polar groups, known to those skilled in the art as glycans. The invention particularly provides novel, poly-amide bonded materials designed for efficient separation of large biomolecules, e.g. materials having a large percentage of larger pores (i.e. wide pores). Furthermore, the invention advantageously provides novel HILIC methods that can be used in combination with the stationary phase materials described herein to effectively separate protein and peptide glycoforms by eliminating previously unsolved problems, such as on-column aggregation of protein samples, low sensitivity of chromatographic detection of the glycan moieties, and low resolution of peaks due to restricted pore diffusion and long intra/inter-particle diffusion distances.

The present disclosure relates to, inter alia, a method of quantitating an amount of an antibody molecule from a mixture comprising two or more antibody molecules, comprising separating each of the two or more antibody molecules from the mixture by hydrophobic interaction chromatography high performance liquid chromatography (HIC-HPLC) and quantitating an amount of each antibody molecule, wherein the molecular weight of each antibody molecule is within 15 kDa of any other antibody molecule in the mixture and either each antibody molecule is different from another antibody molecule in the mixture by more than about 0.25 unit on the Kyte & Doolittle hydropathy scale or each of the antibody molecules when run alone on HIC-HPLC elutes at distinct run time with little overlap from the other antibody molecules in the mixture, or both.

The present disclosure relates to, inter alia, a method of quantitating an amount of an antibody molecule from a mixture comprising two or more antibody molecules, comprising separating each of the two or more antibody molecules from the mixture by hydrophobic interaction chromatography high performance liquid chromatography (HIC-HPLC) and quantitating an amount of each antibody molecule, wherein the molecular weight of each antibody molecule is within 15 kDa of any other antibody molecule in the mixture and either each antibody molecule is different from another antibody molecule in the mixture by more than about 0.25 unit on the Kyte & Doolittle hydropathy scale or each of the antibody molecules when run alone on HIC-HPLC elutes at distinct run time with little overlap from the other antibody molecules in the mixture, or both.

Disclosed are methods for identification of one or more non-native disulfide bonds in a biomolecule (e.g, an antibody). In an example, a method includes performing a digestion of the biomolecule under non-reducing conditions to provide a sample comprising a plurality of biomolecule fragments, contacting the sample to a separation column, applying a first mobile phase gradient comprising trifluoroacetic acid (TFA) and a small molecule additive to the separation column, applying a second mobile phase gradient comprising TFA in acetonitrile (ACN) and a small molecule additive to the separation column, performing a partial reduction procedure on the eluted sample, applying the partially reduced eluted sample components to a mass spectrometer, and performing a mass spectrometric analysis on the partially reduced eluted sample components to identify the one or more non-native disulfide bonds in the biomolecule.