First and second flow-path portions are opposite to each other, and communicate with each other such that a direction in which an eluent flows through the first flow-path portion and a direction in which an eluent flows through the second flow-path portion are opposite to each other. First and second electrode liquid flow paths are respectively opposite to the first and second flow-path portions. First and second electrode liquids are respectively supplied to the first and second electrode liquid flow paths, such that a direction in which the first electrode liquid flows through the first electrode liquid flow path is same as a direction in which an eluent flows through the first flow-path portion and a direction in which the second electrode liquid flows through the second electrode liquid flow path is same as a direction in which an eluent flows through the second flow-path portion.

A new column-based purification system and approach are described for rapid separation and purification of the alpha-emitting therapeutic radioisotope .sup.211At from dissolved cyclotron targets that provide highly reproducible product results with excellent .sup.211At species distributions and high antibody labeling yields compared with prior art manual extraction results of the prior art that can be expected to enable enhanced production of purified .sup.211At isotope products suitable for therapeutic medical applications such as treatment of cancer in human patients.

A method for purifying Ac from a mixture includes Ac and at least one element selected from Ra, Pb, Po, Bi and La. The method includes the steps of: (a) performing a first separation using a first extraction chromatographic column based on a first resin (either a diglycolamide resin or a dialkylphosphoric acid resin) and a first matrix solution; and (b) performing a second separation using a second extraction chromatographic column based on a second resin (respectively either a dialkylphosphoric acid resin or a diglycolamide resin).

The present invention relates to methods of purifying proteins containing Fc regions, such as antibodies and Fc fusion proteins. In particular, the present invention relates to a purification method resulting in reduced levels of aggregate protein comprising adsorbing an Fc region-containing protein to a temperature-responsive protein A resin and eluting the protein from the resin at a temperature below 35 C with an elution buffer comprising a chaotropic agent, a sugar alcohol, and at least one amino acid. Methods of separating fully assembled antibodies from half antibody forms thereof using the elution buffer are also described.

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.

A mobile phase including a lithium salt flows through a stationary phase including an oxygenated metal compound with affinity to the lithium salt through a Lewis acid-Lewis base interaction so that the oxygenated metal compound captures the lithium salt through the Lewis acid-Lewis base interaction. An eluent flows through the stationary phase to release the lithium salt captured by the oxygenated metal compound into the eluent. The eluent includes a Lewis base or a Lewis acid that disrupts the Lewis acid-Lewis base interaction between the lithium salt and the oxygenated metal compound. The eluent including the released lithium salt is collected after the eluent flows through the stationary phase.

Methods for purifying the molybdenum-99 isotope are disclosed. Molybdenum-99 is loaded onto an anion exchange column and extracted. In some embodiments, the extraction solution may include nitric acid and nitrate salts. In other embodiments, a two stage elution is performed in which a nitric acid containing eluent and a hydroxide containing eluent are used in succession to extract molybdenum-99.

Disclosed herein are methods and compositions for isolating a protein fraction from a potato sample. The methods include adjusting the potato sample containing the protein fraction to a pH of about 4.0 to 5.2; and loading the potato sample onto a sulfonated epoxy resin, wherein the sulfonated epoxy resin comprising Formula (I) is adjusted to a pH of about 4.0 to 4.5. The methods also include washing the sulfonated epoxy resin and eluting the protein fraction.

The present disclosure relates to separation and purification methods for a vaccine virus using affinity chromatography, and more particularly, to a purification method for a virus capable of obtaining a vaccine virus with a high purity and a high yield using affinity chromatography containing a vaccine virus-affinity resin.

The present invention provides a chromatographic separation method for improving the quality of albumin fusion protein solutions by removing impurities from the albumin fusion protein solution. This invention provides albumin fusion protein solution with a significantly reduced amount of the (yellow) coloured impurities and HCP.