A method of recovering a sugar by separating a fermentation inhibitor and the sugar from a sugar solution containing the fermentation inhibitor, the method including: bringing the sugar solution containing the fermentation inhibitor into contact with a basic anion exchange resin filled into a column, followed by separation of the fermentation inhibitor and the sugar by a difference in retention time therebetween through use of water as an eluent, and separate recovery of a fraction containing the fermentation inhibitor and a fraction containing the sugar, wherein the basic anion exchange resin is previously treated with a solution containing the fermentation inhibitor.

The present disclosure relates to a method of synthesizing cyclosporine derivatives. The method includes: providing a precursor fluid of the cyclosporine derivative, an alkaline fluid and a ClCH.sub.2OCOCl solution; premixing the precursor fluid and the alkaline fluid to obtain a premixed solution; feeding the premixed solution into a first reaction chamber, reacting to prepare a first reaction liquid; feeding the first reaction liquid into a second reaction chamber, reacting the first reaction liquid with a CO.sub.2 fluid to prepare a second reaction liquid; and reacting the second reaction liquid with the ClCH.sub.2OCOCl solution.

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.

The disclosure discloses a genetically engineered strain for producing porcine myoglobin and fermentation and purification thereof, and belongs to the technical field of genetic engineering. The disclosure realizes efficient secretion and expression of porcine myoglobin by integrating the gene of porcine myoglobin in P. pastoris. On this basis, optimization of the medium and culture conditions of recombinant P. pastoris can significantly increase the titer of porcine myoglobin, so that the titer can reach 285.42 mg/L under fermenter conditions. In addition, by creatively adding different concentrations of ammonium sulfate to fermentation broth step by step, the purity of myoglobin obtained by final concentration is up to 88.0%, and the purification rate is up to 66.1%. The disclosure realizes efficient expression and high purification of porcine myoglobin from various steps such as synthesis, fermentation and purification of porcine myoglobin, and provides broad prospects for industrial production of porcine myoglobin.

Disclosed is a method for efficiently separating and purifying recombinant human coagulate factor VIII Fc fusion protein. The method comprises steps of affinity chromatography and anion exchange chromatography; and the sample captured by means of the affinity chromatography is eluted with a salt ion buffer containing 5%-20% polyol organic solvents under the condition of pH 4.0 to 8.0, and the protein sample can be separated and purified to 85% or more by further ProteinA affinity chromatography. The purification method is simple to operate, naturally connects each step of chromatography, has a high recovery rate and low cost, and easily increases production.

In various aspects, the present disclosure pertains to methods of performing a sample enrichment procedure, which comprise: adding a sample fluid that comprises at least one phospholipid and at least one target analyte to a sorbent that comprises a hydrophobic component and a cation exchange component, thereby resulting in sorbent with bound phospholipid and bound target analyte; adding an aqueous solution comprising an acidic compound and a salt; adding an organic solution to the sorbent thereby desorbing at least a portion of the bound phospholipid from the sorbent; and adding an elution solution to the sorbent, thereby desorbing at least a portion of the bound target analyte from the sorbent and forming a solution of the target analyte in the elution solution. In other aspects, the present disclosure pertains to kits, which may be used in conjunction with such methods.

The present disclosure relates generally to the manufacturing of gene therapy products, and specifically to methods of purifying an enveloped virus from a cell culture fluid, comprising an endonuclease and/or anion exchange chromatography.

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 a hole transport material, a preparation method thereof, and an electroluminescent device. Through ingenious molecular design, a xanthracene structure is combined with different electron-donating groups to synthesize a series of hole transport materials with a suitable highest occupied molecular orbital (HOMO) energy level and a suitable lowest unoccupied molecular orbital (LUMO) energy level, and a series of high-performance display devices can be manufactured using the hole transport materials provided by the present invention.

A process for purification of antibody or fusion protein by affinity chromatography wherein the elution is performed with high salt concentration which reduce turbidity in protein mixture during neutralization steps. The present invention provides an improved process of purifying antibodies through affinity chromatography using high salt-based elution.