The present invention is directed to processes for extracting IgG from an unused waste precipitate produced during normal plasma fractionation processes via a separate fractionation process, thereby increasing the overall yield of IgG from blood plasma.

The present invention relates to a new and improved method for preparing a highly concentrated immunoglobulin composition from pooled plasma for subcutaneous injection. A composition comprising 20% or more immunoglobulin suitable for subcutaneous use is also described.

The present invention relates to the use, for affinity purification of an antibody or an fragment of an antibody, of a ligand-substituted matrix comprising a support material and at least one ligand covalently bonded to the support material, the ligand being represented by formula (I)
L-(Sp).sub.v-Ar.sup.1—Am—Ar.sup.2   (I)
wherein L, SP, Ar.sup.1, AM, Ar.sup.2 and v are defined herein.

The present invention relates to the field of protein purification. In particular, the invention concerns methods for increasing the filtration capacity of virus filters, by combined use of endotoxin removal and cation-exchange media in the prefiltration process.

The present invention relates to the field of antibody formulations. In particular, the present invention relates to specific methods of preparing masked antibodies with reduced aggregation. In some embodiments, the masked antibodies comprise anti-CD47 antibodies.

The present invention provides a downstream purification method process for the production of bispecific antigen-binding polypeptides. The method comprises at least the steps of (i) providing a separation resin comprising a polymer matrix part and a ligand part, wherein the matrix part comprises polymethacrylate and has a particle size of about 30 to 60 pm, wherein the ligand part comprises recombinant protein L, and wherein the ligand part's protein L is covalently bound to the matrix part's particles, (ii) contacting a process fluid comprising the bispecific antigen-binding polypeptide with the separation resin, (iii) capturing the bispecific antigen-binding polypeptide by the ligand part of the separation resin, wherein the bispecific antigen-binding polypeptide reversibly binds to the ligand part of the separation resin, and wherein the remainder of the process fluid does not bind to the ligand part of the separation resin, (iv) washing the bound bispecific antigen-binding polypeptide with a wash buffer which does not elute the bispecific antigen-binding polypeptide from the ligand portion, and (v) elute the bispecific antigen-binding polypeptide from the ligand part with an elution buffer at a low pH.

The present subject matter is directed to a method of manufacturing purified IVIG from Fraction III of plasma, comprising re-constituting a Fraction III paste in a buffer; adjusting the pH and temperature; adding ethanol and then gradually lowering the temperature; centrifuging and filtering the supernatant; ultra-filtrating to remove alcohol; undergoing weak anion exchange chromatography; ultra-filtrating to reach a desired protein concentration; aseptic filtrating; nano filtrating for virus removal; and incubating at low pH for virus inactivation to obtain a resulting Fraction III suspension comprising purified IVIG. The present subject matter is directed to IVIG having 14 newly-found proteins, namely KH 26, KH 27, KH 28, KH 29, KH 30, KH 31, KH 32, KH 33, KH 39, KH 40, KH 41, KH 42, KH 43, and KH 44 for both liquid and lyophilized form.

The present subject matter is directed to a method for separating proteins of plasma using pH adjustment including the steps of reconstituting Fraction III, Fraction IV, or plasma paste, in water for injection; adjusting pH value to 1 and temperature from 1° C. to 30° C.; centrifuging the resulting suspension at 6,000 rpm at 2-8° C. for 20 min; collecting the resulting paste 1 (P1) and supernatant 1 (S1); reconstituting P1 in WFI and adjust the pH to 2; and repeating step 3) to step 5) until the pH of supernatant reaches 14. According to the method, a new formulation of immunoglobulin is prepared from plasma Fraction III and Fraction IV.

The present subject matter is directed to a method of manufacturing and purifying an intravenous injection of prothrombin complex concentration (PCC) from plasma Fraction III and a method of manufacturing and purifying an intravenous injection of non-PCC from plasma Fraction IV. The intravenous injection of PCC and non-PCC obtained from the method can be administered to a patient in need thereof for stopping replication, killing and preventing HIV-1 and HIV-2 in a patient.

Aspects of the disclosure relate to methods of purifying complexes comprising a protein (e.g., antibody) covalently linked to an oligonucleotide. In some embodiments, complexes comprising a protein covalently linked to an oligonucleotide are purified and isolated from unlinked oligonucleotide using an mixed-mode resin that comprises positively-charged metal sites and negatively charged ionic sites, e.g., hydroxyapatite resin. In some embodiments, complexes comprising a protein covalently linked to an oligonucleotide are purified from a mixture comprising the complexes, unlinked protein, and unlinked oligonucleotide using a purification step involving hydrophobic interaction chromatography resin followed by a purification step involving mixed-mode resin.