Methods and systems are provided to improve consistency and robustness in chromatography, for example, in operations of multi-column chromatography systems.

A protein purification process with virus inactivation or removal uses caprylic acid (octanoic acid) at acidic pH. The method comprises caprylic acid treatment as part of the chromatographic step so as to perform viral inactivation without a discontinuous process and without the requirement of attention by personnel, particularly when the pH adjustment of the eluate is performed automatically by eluting into buffer. The method of the invention further results in mycoplasmas being inactivated, and reduced impurities like Host Cell Protein (HCP).

A method for producing 225.sup.A including: a method (X) for purifying a .sup.226Ra-containing solution, including an adsorption step of allowing a .sup.226Ra ion to adsorb onto a carrier having a function of selectively adsorbing a divalent cation by bringing a .sup.226Ra-containing solution into contact with the carrier under an alkaline condition, and an elution step of eluting the .sup.226Ra ion from the carrier under an acidic condition; a method for producing a .sup.226Ra target, including an electrodeposition liquid preparation step of preparing an electrodeposition liquid by using a purified .sup.226Ra-containing solution obtained by the method (X), and an electrodeposition step of electrodepositing a .sup.226Ra-containing substance on a substrate by using the electrodeposition liquid; and a step of irradiating a .sup.226Ra target produced by the method for producing a .sup.226Ra target with at least one selected from a charged particle, a photon, and a neutron by using an accelerator.

A method for purifying a mixture in a multicolumn chromatography system. The method successively and cyclically collects a raffinate, injects the mixture to be separated, collects an extract, and injects eluent. The mixture to be separated contains fructose and has a dry matter mass concentration of 45 to 55%. The method is carried out at a temperature of 50 to 62° C.

Provided herein are methods of separating host cell lipases from an anti-LAG3 antibody or antigen binding fragment in chromatographic processes and methods of improving polysorbate-80 stability in an anti-LAG3 antibody formulation by separating host cell lipases from the anti-LAG3 antibody or antigen binding fragment using chromatographic processes. Also provided are pharmaceutical compositions comprising an anti-LAG3 antibody or antigen binding fragment and less than 2 ppm of a host cell lipase.

A method for removing coloration from a drug substance solution of protein preparation, in particular, antibody preparation, a method for preparing drug substance solution of protein preparations including it, as a part thereof, and highly concentrated, colorless drug substance solutions thereof are disclosed. The method removes terminal glycation products causing the coloration in the drug substance solution of protein preparation, in particular, antibody preparation, by anion-exchange chromatography, making it possible to provide colorless drug substance solutions.

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.

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 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.

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).