The present invention relates to a method and/or device for improving the separation behaviors and performance of aqueous two-phase system (ATPS) for the isolation and/or concentration of one or more target analytes from a sample. In one embodiment, the present method and device comprise ATPS components within a porous material and one or more phase separation behavior modifying agents that improve the separation behavior and performance characteristics of ATPS, including but not limited to the increasing the stability or reducing fluctuations of ATPS thought the adjustment of total volume of a sample solution that undergoes phase separation, volume ratio of the two phases of the ATPS, fluid flow rates, and concentrations of ATPS components.

A process for obtaining soluble functional proteins from plant material includes the steps of: mechanically disrupting the cells of the plant material to obtain a mush stream; subjecting the mush stream to a coarse physical separation step, resulting in a permeate and a retentate; subjecting the permeate P.sub.b to mild treatment, resulting in a treated permeate; subjecting the treated permeate to serial centrifugation steps; subjecting centrate to a microfiltration step resulting in a permeate and a retentate; subjecting the permeate to an ultrafiltration step resulting in a permeate and a retentate; subjecting the retentate to hydrophobic column adsorption to provide a column permeate and a retentate; and drying the column permeate to provide a soluble functional protein isolate.

A process for obtaining soluble functional proteins from plant material includes the steps of: mechanically disrupting the cells of the plant material to obtain a mush stream; subjecting the mush stream to a coarse physical separation step, resulting in a permeate and a retentate; subjecting the permeate P.sub.b to mild treatment, resulting in a treated permeate; subjecting the treated permeate to serial centrifugation steps; subjecting centrate to a microfiltration step resulting in a permeate and a retentate; subjecting the permeate to an ultrafiltration step resulting in a permeate and a retentate; subjecting the retentate to hydrophobic column adsorption to provide a column permeate and a retentate; and drying the column permeate to provide a soluble functional protein isolate.

Disclosed is a method for evaluating in vivo protein nutrition based on an LC-MS-MS technique, including the following steps: (1) collecting contents from different intestinal segments, and extracting and isolating protein ingredients; (2) determining the concentration of proteins; (3) treating before carrying out mass spectrometry: including digestion and desalting of a whole protein solution; (4) LC-MS-MS analysis; (5) database searching; and (6) data processing. Proteomic technology is used to identify proteins in the contents of different intestinal segments and digestive products thereof, and the source of the proteins in the contents of different intestinal segments and the contents thereof can be determined therefrom. Through bioinformatic analysis, the function of differential proteins in the body can be further understood, where the gene expression of enzymes related to protein digestion and metabolism may be different, thereby providing a scientific basis for further scientific evaluation of protein digestion and utilization.

The present invention generally pertains to methods of characterizing charge variants of a protein of interest. In particular, the present invention pertains to the use of desalting size exclusion chromatography-reduced peptide mapping mass spectrometry to identify charge variants separated by capillary isoelectric focusing.

The present invention generally pertains to methods of characterizing charge variants of a protein of interest. In particular, the present invention pertains to the use of desalting size exclusion chromatography-reduced peptide mapping mass spectrometry to identify charge variants separated by capillary isoelectric focusing.

The present invention relates to an improved method of purifying an immunoglobulin, and more particularly to a method of purifying an immunoglobulin which is capable of sufficiently removing impurities from an immunoglobulin-containing plasma protein sample through a simple process, comprising a single anion-exchange chromatography and a single cation-exchange chromatography.

The present invention relates to an improved method of purifying an immunoglobulin, and more particularly to a method of purifying an immunoglobulin which is capable of sufficiently removing impurities from an immunoglobulin-containing plasma protein sample through a simple process, comprising a single anion-exchange chromatography and a single cation-exchange chromatography.

Method and system for purifying a sample comprising a biomolecule of interest and impurities, comprising expressing said biomolecule of interest in a bioreactor to form a product sample comprising said biomolecule of interest and impurities; subjecting said product sample to filtration to form a clarified product sample; subjecting said clarified product sample to affinity chromatography to remove impurities; subsequently subjecting said product sample to diafiltration followed by virus filtration and optional concentration. The buffer used during the diafiltration step (and thus in the virus filtration step) is the buffer desired for the final formulation of the product.

Method and system for purifying a sample comprising a biomolecule of interest and impurities, comprising expressing said biomolecule of interest in a bioreactor to form a product sample comprising said biomolecule of interest and impurities; subjecting said product sample to filtration to form a clarified product sample; subjecting said clarified product sample to affinity chromatography to remove impurities; subsequently subjecting said product sample to diafiltration followed by virus filtration and optional concentration. The buffer used during the diafiltration step (and thus in the virus filtration step) is the buffer desired for the final formulation of the product.