Disclosed herein are methods and exemplary compositions associated with virus purification, antigen purification, and conjugation of virus and proteins (e.g., antigen) to form vaccines for delivery of immunological and other therapeutic agents, exemplary aspects of which may include harvesting viral and antigenic substances from source organisms; a purification platform comprising chemical separation and size-difference separation for the removal of contaminants, debris and impurities from the viral and protein (e.g. antigenic, including influenza hemagglutinin antigens) substances, as well as their concentration and collection; and a conjugation platform providing activation of the virus at a pH that increases binding rate and binding propensity between the virus and the protein, wherein embodiments related to the conjugation platform include controlling the ratio of virus to protein.

The present invention generally pertains to methods of preventing disulfide scrambling in non-reducing liquid chromatography-mass spectrometry analysis of a protein of interest. In particular, the present invention pertains to the addition of cystamine to a non-reducing liquid chromatography-mass spectrometry analysis of an antibody to prevent disulfide scrambling.

The present invention generally pertains to methods of preventing disulfide scrambling in non-reducing liquid chromatography-mass spectrometry analysis of a protein of interest. In particular, the present invention pertains to the addition of cystamine to a non-reducing liquid chromatography-mass spectrometry analysis of an antibody to prevent disulfide scrambling.

Disclosed are methods for critical point drying a composite material. After exposing the composite material to a supercritical fluid, the composite material dries as the supercritical fluid evaporates with reduced pressure. The composite materials are useful as chromatographic separation media.

A process for purifying a recombinant protein comprising the steps of: i) providing a solution comprising the recombinant protein; ii) adding an alkyl glycoside to the solution; and iii) purifying the recombinant protein. The addition of the alkyl glycoside provides improved clearance of process-related impurities. The purified recombinant protein of the invention has low levels of host cell DNA, host cell protein and viral contamination.

A process for purifying a composition comprising water, a target substance, impurities and optionally cells, the process comprising the steps (A) and (B): (A) preparing a liquid feedstock by performing step (Ai) and/or (Aii) on the composition: (Ai) removing at least some of the cells from the composition; (Aii) concentrating the composition by removing water therefrom; and (B) passing the liquid feedstock through an apparatus comprising at least two processing units, each such unit producing a product stream containing purified target substance and optionally a waste stream comprising at least some of the impurities, wherein each unit comprises specified components (i) to (v). The units may be essentially the same except for a device they contain, leading to advantages in terms of simplicity, cost and ease of operation, lower risk of operator error, easier maintenance and lower inventory of spare parts.

An Fc-binding protein exhibiting improved alkaline resistance, a method for producing the protein, an antibody adsorbent obtained by immobilizing the protein on a carrier, and a method for separating an antibody using the adsorbent.

An Fc-binding protein exhibiting improved alkaline resistance, a method for producing the protein, an antibody adsorbent obtained by immobilizing the protein on a carrier, and a method for separating an antibody using the adsorbent.

The present disclosure provides methods for producing consumable recombinant proteins that are substantially free from herein-disclosed undesired byproducts.

The present disclosure provides methods for producing consumable recombinant proteins that are substantially free from herein-disclosed undesired byproducts.