# US 2009/0269359 A1 · Method of Treatment and Prophylaxis of Diseases Related to Amyloid Deposition Using IGM > Agents: this data is available as JSON from the patentgrep API and MCP server — see https://patentgrep.com/llms.txt - Number: US 2009/0269359 A1 - Document ID: US20090269359A1 - Status: Published application - Kind: A1 - Application number: 12/162,532 - Filed: 2007-01-30 - Published: 2009-10-29 - Earliest claimed: 2006-01-30 - Assignees: Talecris Biotherapeutics, Inc. - Inventors: Philip Scuderi, JR.; Afshin Safavi; Matthew G. Langevin - Web page: https://patentgrep.com/patent/US20090269359A1 ## CPC - C07K 16/065: {Purification, fragmentation} - A61K 39/39591: {Stabilisation, fragmentation} - A61P 7/00: Drugs for disorders of the blood or the extracellular fluid - A61P 13/12: of the kidneys - A61P 21/00: Drugs for disorders of the muscular or neuromuscular system - A61P 25/00: Drugs for disorders of the nervous system - A61P 25/28: for treating neurodegenerative disorders of the central nervous system, e.g. nootropic agents, cognition enhancers, drugs for treating Alzheimer's disease or other forms of dementia - A61P 29/00: Non-central analgesic, antipyretic or antiinflammatory agents, e.g. antirheumatic agents; Non-steroidal antiinflammatory drugs [NSAID] - A61P 35/00: Antineoplastic agents - A01K 2267/0312: Animal model for Alzheimer's disease - A61K 2039/505: {comprising antibodies} - C07K: PEPTIDES (peptides in foodstuffs A23; obtaining protein compositions for foodstuffs, working-up proteins for foodstuffs A23J; preparations for medicinal purposes A61K; peptides containing beta-lactam rings C07D; cyclic dipeptides not having in their molecule any other peptide link than those which form their ring, e.g. piperazine-2,5-diones, C07D; ergot alkaloids of the cyclic peptide type C07D519/02; macromolecular compounds having statistically distributed amino acid units in their molecules, i.e. when the preparation does not provide for a specific; but for a random sequence of the amino acid units, homopolyamides and block copolyamides derived from amino acids C08G69/00; macromolecular products derived from proteins C08H1/00; preparation of glue or gelatine C09H; single cell proteins, enzymes C12N; genetic engineering processes for obtaining peptides C12N15/00; compositions for measuring or testing processes involving enzymes C12Q; investigation or analysis of biological material G01N33/00) - A61K: PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES (devices or methods specially adapted for bringing pharmaceutical products into particular physical or administering forms A61J3/00; chemical aspects of, or use of materials for deodorisation of air, for disinfection or sterilisation, or for bandages, dressings, absorbent pads or surgical articles A61L; soap compositions C11D) - A61P: SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS - A01K: ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS ## Abstract The invention relates to a method of treating or preventing disease associated with β-amyloid polypeptides comprising administration of an immunoglobulin preparation enriched in immunoglobulin M (IgM), and pharmaceutical compositions comprising such preparations. ## Claims ### Claim 1 A method of treating or preventing a disease associated with β-amyloid polypeptides comprising administration of an immunoglobulin preparation produced from pooled human plasma samples as starting material, wherein the immunoglobulin preparation is enriched in immunoglobulin M (IgM). ### Claim 2 (depends on 1) The method of claim 1, wherein the immunoglobulin preparation comprises at least about 80% IgM or at least about 90% IgM. ### Claim 3 (depends on 1) The method of claim 1, wherein the immunoglobulin preparation comprises IgM antibodies that bind specifically to Aβ 1-42. ### Claim 4 (depends on 1) The method of claim 1, wherein the disease associated with β-amyloid polypeptides is selected from the group consisting of chronic inflammatory illnesses, multiple myeloma, macroglobulinernia, familial amyloid polyneuropathy (Portuguese) and cardiomyopathy (Danish), systemic senile amyloidosis, familial amyloid polynephropathy (Iowa), familial amyloidosis (Finnish), Gerstmann-Straussler-Scheinker syndrome, familial amyloid nephropathy with urticaria and deafness (Muckle-Wells syndrome), medullary carcinoma of thyroid, isolated atrial amyloid, and hemodialysis-associated amyloidosis (HAA), sporadic cerebral amyloid angiopathy, hereditary cerebral amyloid angiopathy, Downs syndrome, Parkinson-dementia of Guam, age-related asymptomatic amyloid angiopathy, hereditary cerebral hemorrhage with amyloidosis, and Alzheimer's disease. ### Claim 5 (depends on 1) The method of claim 1, wherein the disease associated with β-amyloid polypeptides is an amyloid-associated neurodegenerative disease. ### Claim 6 (depends on 5) The method of claim 5, wherein the disease is Alzheimer's disease. ### Claim 7 (depends on 1) The method of claim 1, wherein the immunoglobulin preparation is administered at a dosage of immunoglobulin from about 0.1 μg per kg body weight to about 1000 mg per kg body weight. ### Claim 8 (depends on 1) The method of claim 1, wherein the immunoglobulin preparation is administered at a dosage of from about 0.5 μg per kg body weight to about 500 mg per kg body weight; from about 0.5 μg per kg body weight to about 100 mg per kg body weight; or from about 5 μg per kg body weight to about 50 mg per kg body weight. ### Claim 9 A pharmaceutical composition comprising IgM, at least a portion of which binds specifically to Aβ 1-42, where the IgM is prepared from starting material comprising immunoglobulins and other substances by a) adjusting the pH of the starting material to form an intermediate solution comprising dissolved immunoglobulins, b) adjusting the intermediate solution of step a) to conditions of pH, temperature, and caprylate concentration such that a first precipitate and a first supernatant comprising immunoglobulins are formed, c) separating the first supernatant from the first precipitate, d) incubating the first supernatant under conditions of time, pH, temperature and caprylate concentration such that a second precipitate and a second supernatant comprising immunoglobulins are formed, e) separating the second supernatant from the second precipitate, f) contacting the second supernatant with a first anion exchange resin under conditions of pH and ionic strength such that substantially none of the immunoglobulin G or immunoglobulin M is bound to the first resin but immunoglobulin A and other substances are bound to the first resin, g) separating a fraction containing substantially all of the immunoglobulin G and immunoglobulin M from the result of the previous step, h) contacting the immunoglobulin G and M with a second anion exchange resin under conditions of pH and ionic strength such that substantially none of the immunoglobulin G is bound to the second resin but immunoglobulin M and other substances are bound to the second resin, i) eluting IgM from the second anion exchange resin column with a buffered solution having a conductivity in the range of that found in a solution of at least 100 mM sodium chloride, j) applying the IgM to a gel filtration resin and recovering the IgM, k) applying the IgM to an affinity resin comprising immobilized antigens A and B, and l) recovering the IgM. ### Claim 10 (depends on 9) The pharmaceutical composition of claim 9, wherein the starting material is derived from pooled human blood products. ### Claim 11 (depends on 10) The pharmaceutical composition of claim 10, wherein pooled human blood products are collected from donors that have not been screened to determine their anti-Aβ immunoglobulin titer.