Combinations of different chromatography modalities with particularly refined conditions significantly reduce acid charge variants in a preparation of monoclonal antibodies. The process for reducing acid charge variants utilizes a combination of anion exchange and hydrophobic interaction chromatography, followed by cation exchange chromatography polishing, whereby the levels of acidic or basic charge species of the monoclonal antibodies may be modulated to a desired level.

Combinations of different chromatography modalities with particularly refined conditions significantly reduce acid charge variants in a preparation of monoclonal antibodies. The process for reducing acid charge variants utilizes a combination of anion exchange and hydrophobic interaction chromatography, followed by cation exchange chromatography polishing, whereby the levels of acidic or basic charge species of the monoclonal antibodies may be modulated to a desired level.

A process for producing an arginine-rich peptide mixture and the application thereof in cervical cancer therapy is provided. The process includes the following steps: A suspension of walnut meal and egg albumin is pretreated with ultrahigh pressure, and then digested by alkaline proteinase and papain in separated steps with the ultrasonic and microwave-assisted extraction. The peptides of interest are isolated from filtration supernatant obtained after the enzyme digestion by reversed phase high-performance liquid chromatography. By using the peptide mixture as a template, acrylic acid and methyl acrylic acid as functional monomers, triethylene glycol dimethacrylate as cross-linking agent, and isopropylthioxanthone in acetone as a photoinitiator, polymerization is induced by ultraviolet light to form a surface imprinted membrane for isolating and enriching the peptides of interest from the supernatant. The arginine content in the peptide mixture is more than 18%. The arginine-rich peptide mixture is able to strongly suppress the proliferation of human cervical cancer Hela cells. The approach is applicable to reduce the cost of production and speed up the commercialization of large-scale production.

A process for producing an arginine-rich peptide mixture and the application thereof in cervical cancer therapy is provided. The process includes the following steps: A suspension of walnut meal and egg albumin is pretreated with ultrahigh pressure, and then digested by alkaline proteinase and papain in separated steps with the ultrasonic and microwave-assisted extraction. The peptides of interest are isolated from filtration supernatant obtained after the enzyme digestion by reversed phase high-performance liquid chromatography. By using the peptide mixture as a template, acrylic acid and methyl acrylic acid as functional monomers, triethylene glycol dimethacrylate as cross-linking agent, and isopropylthioxanthone in acetone as a photoinitiator, polymerization is induced by ultraviolet light to form a surface imprinted membrane for isolating and enriching the peptides of interest from the supernatant. The arginine content in the peptide mixture is more than 18%. The arginine-rich peptide mixture is able to strongly suppress the proliferation of human cervical cancer Hela cells. The approach is applicable to reduce the cost of production and speed up the commercialization of large-scale production.

The present disclosure pertains to compositions comprising anti-VEGF proteins.

The present disclosure pertains to compositions comprising anti-VEGF proteins.

The present invention provides a novel process of PEGylation and purification of the PEGylated therapeutic proteins. The developed PEGylation protocol provides high yield of PEGylated recombinant proteins (with % mono-PEG conversion of ≥70%) with a much faster reaction completion time indicating high productivity and fast kinetics. Thereafter a displacement mode cation exchange chromatography (CEX) is utilized which is able to remove all the multi-PEGylated impurities in the loading flow-through, simplifying the overall purification process. The novel PEGylation and purification process can be integrated to any existing manufacturing process to offer an end-to-end integrated assembly from inclusion bodies to purified PEGylated product with higher productivity and improved resin utilization.

The present invention provides a novel process of PEGylation and purification of the PEGylated therapeutic proteins. The developed PEGylation protocol provides high yield of PEGylated recombinant proteins (with % mono-PEG conversion of ≥70%) with a much faster reaction completion time indicating high productivity and fast kinetics. Thereafter a displacement mode cation exchange chromatography (CEX) is utilized which is able to remove all the multi-PEGylated impurities in the loading flow-through, simplifying the overall purification process. The novel PEGylation and purification process can be integrated to any existing manufacturing process to offer an end-to-end integrated assembly from inclusion bodies to purified PEGylated product with higher productivity and improved resin utilization.

Rapid, animal protein free, chromatographic processes and systems for obtaining high potency, high yield botulinum neurotoxin for research, therapeutic and cosmetic use.

Rapid, animal protein free, chromatographic processes and systems for obtaining high potency, high yield botulinum neurotoxin for research, therapeutic and cosmetic use.