Systems and methods for characterizing low molecular weight (LMW) protein drug product impurities are provided. One embodiment uses hydrophilic interaction chromatography (HILIC) coupled to mass spectrometry analysis. After removal of the N-linked glycans from the protein drug product, for example an antibody drug product, the elution of LMW impurities from the HILIC column was determined by the size of the molecular weight species. In some embodiments, the HILIC separation is performed under denaturing conditions, making the detection of LMW forms using this method highly comparable to both SDS-PAGE and CE-SDS methods. LMW drug product impurities include, but are not limited to light chain, half antibody, H2L, H2, HL, HC, peptide backbone-truncated species, and combinations thereof.

The present disclosure discloses a method for accurately separating and identifying an oxidized triglyceride in frying oil, and belongs to the technical field of detection. In the present disclosure, the structure of the oxidized triglyceride (ox-TG) in the frying oil is identified by mass spectrometry first. It is found that after frying is conducted for 24 h, the ox-TG mainly includes epoxy ox-TG, hydroxyl ox-TG, and aldehyde ox-TG. Thus, the three types of ox-TG are selected as a template molecule to synthesize a surface molecularly imprinted polymer (SMIPs). Then, a polymer completely matched with the ox-TG template molecule in action site and spatial configuration is synthesized, and the specific ox-TG can be separated by using the SMIPs. According to the present disclosure, OXTG-SMIPs prepared by a molecular imprinting technology has good specificity, stability, and affinity, and accurate separation of the ox-TG in the frying oil can be achieved.

A method for the manufacture of highly purified .sup.68Ge material for radiopharmaceutical purposes. The invention particularly concerns the production of .sup.68Ge-API (API=Active Pharmaceutical Ingredient) solution complying with the Guidelines for good manufacturing practices (GMP). Starting material for the method of the present invention can be a .sup.68Ge stock solution of commercial or other origin as raw material. Such .sup.68Ge containing raw solutions are purified from potential metal and organic impurities originating from production processes. The radiochemical method disclosed is based on a twofold separation of .sup.68Ge from organic and metallic impurities with two different adsorbent materials. During the first separation phase .sup.68Ge is purified from both organic and metallic impurities by adsorption in germanium tetrachloride form, after which hydrolyzed .sup.68Ge is purified from remaining metallic impurities by cation exchange. The final .sup.68Ge-API-product e.g. fulfills the regulatory requirements for specifications of the GMP production of .sup.68Ge/.sup.68Ga generators.

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.

A composition includes a hybrid ligand. The hybrid ligand includes an amine group, an amide group or a sulfonamide group, and hydroxyl groups. A first method includes providing a solution containing a first polar analyte and a second polar analyte, applying the solution to a stationary phase including an immobilized hybrid ligand, applying an elution solvent to the stationary phase such that the first polar analyte and the second polar analyte pass through the stationary phase with different elution times, and collecting the first polar analyte at a first elution time and collecting the second polar analyte at a second elution time after the first elution time. A device of a packed column, a cartridge, a tube, a well plate, a membrane, or a planar thin-layer chromatography plate includes a solid support and a hybrid ligand coupled to the solid support. A second method forms an immobilized hybrid ligand.

Substantially pure saponin extracts and orthogonal chromatographic methods for purification of saponin extracts are disclosed. The purified saponin extracts may include QS-21 and can have a purity of greater than 97%. The orthogonal chromatographic method uses reversed-phase (RP) chromatography followed by hydrophilic interaction liquid chromatography (HILIC) to generate substantially pure saponin extracts.

Substantially pure saponin extracts and orthogonal chromatographic methods for purification of saponin extracts are disclosed. The purified saponin extracts may include QS-21 and can have a purity of greater than 97%. The orthogonal chromatographic method uses reversed-phase (RP) chromatography followed by hydrophilic interaction liquid chromatography (HILIC) to generate substantially pure saponin extracts.

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.

A method of purification and/or separation of glycopeptides and quantitation of same. The method includes contacting a sample comprising glycopeptides to a hydrophilic enrichment substrate under conditions that permit the glycopeptides to bind to the hydrophilic enrichment substrate. The glycopeptides are eluted from the hydrophilic enrichment substrate with an ammonium formate and acetonitrile (ACN) in water solution to create an enriched glycopeptide sample, which may be subjected to analysis to identify specific glycopeptides.

Methods for identifying viral protein constituents and quantifying the relative abundance of such viral protein constituents in a sample of viral particles are disclosed. In embodiments, the methods include first-dimension chromatography to separate intact viral capsid components of the sample, online denaturation of the viral capsid components to produce intact viral proteins, second-dimension chromatography to separate the viral proteins, and mass spectrometry to determine the masses of the viral proteins and identify the viral protein constituents of the sample.