The present invention relates to a method for an improved preparative separation of proteins, particularly monoclonal antibodies (mAB) from its associated charge variants (e. g. acidic and basic monomers), glycosylation variants, and/or soluble size variants (e. g. aggregates, monomers, fragments, fragments, antigen binding fragments (Fab) and crystallisable fragments (Fc).

The present disclosure relates to the detection of analytes in high volumetric flow applications. Particular embodiments relate to the use of fluorescence polarization/anisotropy based for detection of analytes in a flow cell. In one testing format, an analyte of interest is probed with reagents containing fluorescent labeled recognition elements. When present in a sample or portion of a sample, the labeled analyte produces a shift in fluorescence polarization/anisotropy/intensity/lifetime as the output signal following the binding of the recognition elements to the analytes.

The present disclosure relates to the detection of analytes in high volumetric flow applications. Particular embodiments relate to the use of fluorescence polarization/anisotropy based for detection of analytes in a flow cell. In one testing format, an analyte of interest is probed with reagents containing fluorescent labeled recognition elements. When present in a sample or portion of a sample, thee labeled analyte produces a shift in fluorescence polarization/anisotropy/intensity/lifetime as the output signal following the binding of the recognition elements to the analytes.

A chromatography medium comprising porous beads having an inner porous core and an outer porous shell is used for chromatographic separation of enveloped or membranous biological particles from impurities such as contaminant DNA and/or protein. The core is capable of binding molecules via hydrophobic interactions; however, the pore size of the shell does not allow particles having a size of 20 nm and larger to permeate into the bead and interact with the core. The separation is performed at a pH of less than 7.4. The enveloped or membranous biological particles may have been subjected to a prior chromatographic capture step. When used for purification of enveloped virus particles the inventive process was found to yield a remarkably high rate of infectious virus particles.

The invention discloses a method for the detection of sialate glycosyl casein glycomacropeptide by boronate affinity column enrichment-liquid chromatography-tandem mass spectrometry using phenylboric acid modified mesoporous silica as packing material, which belongs to the field of food analysis and detection. The method includes the following steps: (1) sample preparation; (2) enrichment and purification of boronate affinity column; (3) liquid chromatography-tandem mass spectrometry detection. The invention makes use of the affinity property of phenylboric acid to the special sugar group sialic acid on the serine and threonine residues in casein glycogiant peptide, regulates the adsorption and elution of casein glycogiant peptide with sialic acid group by changing pH. Combined with the high sensitivity and accuracy of liquid chromatography tandem mass spectrometry, it can be used for qualitative and quantitative analysis of casein glycomacropeptide with sialate glycol-group in phenylketonuria special medical formulations with complex matrix.