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.

The present disclosure pertains to sample preparation devices useful for affinity capture and purification that include one or more internal structures that comprise a reservoir, a well, a fluid passageway, sorbent particles, and a filter element that blocks passage of the affinity sorbent particles, which sample preparation devices combine the attributes of both dispersive and flow through designs into a single sample preparation device. The present disclosure also pertains to kits that contain and methods that use such sample preparation devices.

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.

New metrics are disclosed for characterizing polyethylene copolymers which can be computed from the Cross-Fractionation Chromatography data of these polymers. These metrics are able to quantify the Broad Orthogonal Composition Distribution (BOCD) character of the polymers, and they can be used to discriminate polymers with an enhanced BOCD character from polymers that have the BOCD character to a lesser extent or from polymers that have the conventional molecular weight distribution and/or branching distribution.

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.

The present invention describes a simple purification process for recombinant human serum albumin. The process results in highly purified protein with limited number of purification steps. The broth containing human albumin is clarified by centrifugation and microfiltration, diafiltered and captured by cation exchange chromatography by a process that allows 140-230 mg of albumin to be captured per mi of resin. Product related impurities are removed by hydrophobic interaction chromatography, optimised to allow 87-97% recovery in flow through mode. The final series of processes are so combined that there is easy transition from one step to the next with minimal interventions and adjustments. The entire process of purification is completed within two days from harvest to final product. Thus a cost-effective process with improved recovery of protein at each step is developed. The purified human serum albumin is analyzed for purity and shows physicochemical characteristics that are similar to standard albumin.

A process for isolating astatine includes (a) contacting a composition comprising astatine and bismuth with nitric acid to form a first solution comprising astatine, bismuth, and nitric acid; (b) contacting a resin with the first solution so that astatine partitions out of the first solution and into the resin; and (c) eluting astatine from the resin. A composition comprising astatine may be of the formula AtO.sup.+X.sup.−, wherein X.sup.− is a counterion.

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.

The present invention relates to a preparative chromatography system (200, 500, 800) and a chromatography process (400, 700) adapted to repetitive cycling of chromatography volumes. The system (200, 500, 800) comprises at least two upstream pumps (203a, 803a, 203b, 803b) and separate flow paths (220) from process liquid sources to the chromatography device (200, 500, 800). The system (200, 500, 800) is arranged to prime one flow path (220) with one process liquid while providing another process liquid to the chromatography device and thereby minimizing the hold-up volume of the system (200, 500, 800).