SK288128B6 - Process for purifying immunoglobulin G (IgG), liquid immunoglobulin product and use thereof for the preparation of a medicament - Google Patents
Process for purifying immunoglobulin G (IgG), liquid immunoglobulin product and use thereof for the preparation of a medicament Download PDFInfo
- Publication number
- SK288128B6 SK288128B6 SK1866-2000A SK18662000A SK288128B6 SK 288128 B6 SK288128 B6 SK 288128B6 SK 18662000 A SK18662000 A SK 18662000A SK 288128 B6 SK288128 B6 SK 288128B6
- Authority
- SK
- Slovakia
- Prior art keywords
- immunoglobulin
- igg
- exchange resin
- product
- buffer
- Prior art date
Links
- 229940027941 immunoglobulin g Drugs 0.000 title claims abstract description 165
- 238000000034 method Methods 0.000 title claims abstract description 100
- 238000002360 preparation method Methods 0.000 title claims abstract description 39
- 230000008569 process Effects 0.000 title claims abstract description 36
- 239000007788 liquid Substances 0.000 title claims abstract description 27
- 239000003814 drug Substances 0.000 title claims abstract description 13
- 108060003951 Immunoglobulin Proteins 0.000 title claims description 116
- 102000018358 immunoglobulin Human genes 0.000 title claims description 116
- 239000000047 product Substances 0.000 claims abstract description 126
- 241000700605 Viruses Species 0.000 claims abstract description 89
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 75
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 75
- 239000000872 buffer Substances 0.000 claims abstract description 49
- 239000003729 cation exchange resin Substances 0.000 claims abstract description 33
- NWUYHJFMYQTDRP-UHFFFAOYSA-N 1,2-bis(ethenyl)benzene;1-ethenyl-2-ethylbenzene;styrene Chemical compound C=CC1=CC=CC=C1.CCC1=CC=CC=C1C=C.C=CC1=CC=CC=C1C=C NWUYHJFMYQTDRP-UHFFFAOYSA-N 0.000 claims abstract description 29
- 239000003957 anion exchange resin Substances 0.000 claims abstract description 23
- 230000000415 inactivating effect Effects 0.000 claims abstract description 23
- 238000011026 diafiltration Methods 0.000 claims abstract description 21
- 239000006228 supernatant Substances 0.000 claims abstract description 21
- 238000000108 ultra-filtration Methods 0.000 claims abstract description 18
- 239000000356 contaminant Substances 0.000 claims abstract description 15
- 239000000178 monomer Substances 0.000 claims abstract description 14
- 238000011282 treatment Methods 0.000 claims abstract description 13
- 108010058237 plasma protein fraction Proteins 0.000 claims abstract description 8
- 229940081857 plasma protein fraction Drugs 0.000 claims abstract description 8
- 238000005406 washing Methods 0.000 claims abstract description 6
- 241000124008 Mammalia Species 0.000 claims abstract description 4
- 239000000243 solution Substances 0.000 claims description 52
- 239000002202 Polyethylene glycol Substances 0.000 claims description 41
- 229920001223 polyethylene glycol Polymers 0.000 claims description 41
- 238000010828 elution Methods 0.000 claims description 33
- 239000003381 stabilizer Substances 0.000 claims description 33
- 238000001556 precipitation Methods 0.000 claims description 26
- 239000003599 detergent Substances 0.000 claims description 24
- 239000000725 suspension Substances 0.000 claims description 24
- 239000003795 chemical substances by application Substances 0.000 claims description 21
- 229920000642 polymer Polymers 0.000 claims description 20
- 108010088751 Albumins Proteins 0.000 claims description 19
- 102000009027 Albumins Human genes 0.000 claims description 19
- 229940072221 immunoglobulins Drugs 0.000 claims description 19
- 239000000203 mixture Substances 0.000 claims description 19
- 125000002057 carboxymethyl group Chemical group [H]OC(=O)C([H])([H])[*] 0.000 claims description 17
- 239000002245 particle Substances 0.000 claims description 15
- 230000003612 virological effect Effects 0.000 claims description 15
- 229920002684 Sepharose Polymers 0.000 claims description 14
- 238000005277 cation exchange chromatography Methods 0.000 claims description 13
- 239000000539 dimer Substances 0.000 claims description 13
- 239000000126 substance Substances 0.000 claims description 13
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 claims description 12
- 238000005571 anion exchange chromatography Methods 0.000 claims description 12
- 239000011347 resin Substances 0.000 claims description 12
- 229920005989 resin Polymers 0.000 claims description 12
- 239000002904 solvent Substances 0.000 claims description 12
- 208000011580 syndromic disease Diseases 0.000 claims description 12
- 102000004506 Blood Proteins Human genes 0.000 claims description 11
- 108010017384 Blood Proteins Proteins 0.000 claims description 11
- 229920002271 DEAE-Sepharose Polymers 0.000 claims description 10
- 238000005349 anion exchange Methods 0.000 claims description 9
- 206010021245 Idiopathic thrombocytopenic purpura Diseases 0.000 claims description 8
- 208000031951 Primary immunodeficiency Diseases 0.000 claims description 8
- -1 diethylaminoethyl groups Chemical group 0.000 claims description 8
- 206010054979 Secondary immunodeficiency Diseases 0.000 claims description 7
- 239000007900 aqueous suspension Substances 0.000 claims description 7
- 201000001320 Atherosclerosis Diseases 0.000 claims description 6
- FGUUSXIOTUKUDN-IBGZPJMESA-N C1(=CC=CC=C1)N1C2=C(NC([C@H](C1)NC=1OC(=NN=1)C1=CC=CC=C1)=O)C=CC=C2 Chemical compound C1(=CC=CC=C1)N1C2=C(NC([C@H](C1)NC=1OC(=NN=1)C1=CC=CC=C1)=O)C=CC=C2 FGUUSXIOTUKUDN-IBGZPJMESA-N 0.000 claims description 6
- 108010032597 Cohn fraction II Proteins 0.000 claims description 6
- 239000008118 PEG 6000 Substances 0.000 claims description 6
- 229920002584 Polyethylene Glycol 6000 Polymers 0.000 claims description 6
- 206010040070 Septic Shock Diseases 0.000 claims description 6
- 239000013578 denaturing buffer Substances 0.000 claims description 6
- 238000001990 intravenous administration Methods 0.000 claims description 6
- WWZKQHOCKIZLMA-UHFFFAOYSA-N octanoic acid Chemical compound CCCCCCCC(O)=O WWZKQHOCKIZLMA-UHFFFAOYSA-N 0.000 claims description 6
- 239000002244 precipitate Substances 0.000 claims description 6
- 239000011780 sodium chloride Substances 0.000 claims description 6
- 206010036105 Polyneuropathy Diseases 0.000 claims description 5
- 239000008351 acetate buffer Substances 0.000 claims description 5
- 229940023913 cation exchange resins Drugs 0.000 claims description 5
- 230000036425 denaturation Effects 0.000 claims description 5
- 238000004925 denaturation Methods 0.000 claims description 5
- GNFTZDOKVXKIBK-UHFFFAOYSA-N 3-(2-methoxyethoxy)benzohydrazide Chemical compound COCCOC1=CC=CC(C(=O)NN)=C1 GNFTZDOKVXKIBK-UHFFFAOYSA-N 0.000 claims description 4
- 229920002562 Polyethylene Glycol 3350 Polymers 0.000 claims description 4
- 229920001030 Polyethylene Glycol 4000 Polymers 0.000 claims description 4
- 206010037549 Purpura Diseases 0.000 claims description 4
- 241001672981 Purpura Species 0.000 claims description 4
- 150000001413 amino acids Chemical class 0.000 claims description 4
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 claims description 4
- 229910052921 ammonium sulfate Inorganic materials 0.000 claims description 4
- 235000011130 ammonium sulphate Nutrition 0.000 claims description 4
- 230000001684 chronic effect Effects 0.000 claims description 4
- 239000012141 concentrate Substances 0.000 claims description 4
- 230000007824 polyneuropathy Effects 0.000 claims description 4
- 239000007787 solid Substances 0.000 claims description 4
- 235000000346 sugar Nutrition 0.000 claims description 4
- 150000008163 sugars Chemical class 0.000 claims description 4
- 206010055128 Autoimmune neutropenia Diseases 0.000 claims description 3
- 208000035143 Bacterial infection Diseases 0.000 claims description 3
- 239000005635 Caprylic acid (CAS 124-07-2) Substances 0.000 claims description 3
- 206010008874 Chronic Fatigue Syndrome Diseases 0.000 claims description 3
- 206010009900 Colitis ulcerative Diseases 0.000 claims description 3
- 206010056370 Congestive cardiomyopathy Diseases 0.000 claims description 3
- 208000011231 Crohn disease Diseases 0.000 claims description 3
- 201000010046 Dilated cardiomyopathy Diseases 0.000 claims description 3
- 208000003456 Juvenile Arthritis Diseases 0.000 claims description 3
- 206010059176 Juvenile idiopathic arthritis Diseases 0.000 claims description 3
- 201000004681 Psoriasis Diseases 0.000 claims description 3
- 208000021386 Sjogren Syndrome Diseases 0.000 claims description 3
- 206010044248 Toxic shock syndrome Diseases 0.000 claims description 3
- 231100000650 Toxic shock syndrome Toxicity 0.000 claims description 3
- 201000006704 Ulcerative Colitis Diseases 0.000 claims description 3
- 208000006673 asthma Diseases 0.000 claims description 3
- 230000001363 autoimmune Effects 0.000 claims description 3
- 208000022362 bacterial infectious disease Diseases 0.000 claims description 3
- 208000019069 chronic childhood arthritis Diseases 0.000 claims description 3
- 206010012601 diabetes mellitus Diseases 0.000 claims description 3
- 206010014665 endocarditis Diseases 0.000 claims description 3
- 201000002215 juvenile rheumatoid arthritis Diseases 0.000 claims description 3
- 206010065579 multifocal motor neuropathy Diseases 0.000 claims description 3
- 201000006417 multiple sclerosis Diseases 0.000 claims description 3
- 208000029766 myalgic encephalomeyelitis/chronic fatigue syndrome Diseases 0.000 claims description 3
- 206010028417 myasthenia gravis Diseases 0.000 claims description 3
- 229960002446 octanoic acid Drugs 0.000 claims description 3
- 230000002093 peripheral effect Effects 0.000 claims description 3
- 230000036303 septic shock Effects 0.000 claims description 3
- 201000009890 sinusitis Diseases 0.000 claims description 3
- 239000011534 wash buffer Substances 0.000 claims description 3
- 208000030507 AIDS Diseases 0.000 claims description 2
- 108091006027 G proteins Proteins 0.000 claims description 2
- 102000030782 GTP binding Human genes 0.000 claims description 2
- 108091000058 GTP-Binding Proteins 0.000 claims description 2
- 208000008899 Habitual abortion Diseases 0.000 claims description 2
- 201000010743 Lambert-Eaton myasthenic syndrome Diseases 0.000 claims description 2
- 206010028424 Myasthenic syndrome Diseases 0.000 claims description 2
- 208000003435 Optic Neuritis Diseases 0.000 claims description 2
- YTAHJIFKAKIKAV-XNMGPUDCSA-N [(1R)-3-morpholin-4-yl-1-phenylpropyl] N-[(3S)-2-oxo-5-phenyl-1,3-dihydro-1,4-benzodiazepin-3-yl]carbamate Chemical compound O=C1[C@H](N=C(C2=C(N1)C=CC=C2)C1=CC=CC=C1)NC(O[C@H](CCN1CCOCC1)C1=CC=CC=C1)=O YTAHJIFKAKIKAV-XNMGPUDCSA-N 0.000 claims description 2
- 230000001476 alcoholic effect Effects 0.000 claims description 2
- 235000001014 amino acid Nutrition 0.000 claims description 2
- 208000007502 anemia Diseases 0.000 claims description 2
- BNMJSBUIDQYHIN-UHFFFAOYSA-N butyl dihydrogen phosphate Chemical compound CCCCOP(O)(O)=O BNMJSBUIDQYHIN-UHFFFAOYSA-N 0.000 claims description 2
- 239000003153 chemical reaction reagent Substances 0.000 claims description 2
- 238000011118 depth filtration Methods 0.000 claims description 2
- 206010015037 epilepsy Diseases 0.000 claims description 2
- 230000002757 inflammatory effect Effects 0.000 claims description 2
- 208000004235 neutropenia Diseases 0.000 claims description 2
- 208000006473 polyradiculopathy Diseases 0.000 claims description 2
- 206010061928 radiculitis Diseases 0.000 claims description 2
- 230000003253 viricidal effect Effects 0.000 claims description 2
- 102000054765 polymorphisms of proteins Human genes 0.000 claims 2
- 206010061218 Inflammation Diseases 0.000 claims 1
- 230000004054 inflammatory process Effects 0.000 claims 1
- 238000001914 filtration Methods 0.000 abstract description 8
- 201000010099 disease Diseases 0.000 abstract description 5
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 abstract description 5
- 230000001376 precipitating effect Effects 0.000 abstract description 4
- 230000007812 deficiency Effects 0.000 abstract description 3
- 230000003297 denaturating effect Effects 0.000 abstract 1
- 235000018102 proteins Nutrition 0.000 description 67
- 229940008228 intravenous immunoglobulins Drugs 0.000 description 50
- 101150026046 iga gene Proteins 0.000 description 30
- 230000000694 effects Effects 0.000 description 28
- 210000002381 plasma Anatomy 0.000 description 21
- 230000002779 inactivation Effects 0.000 description 19
- OWEGMIWEEQEYGQ-UHFFFAOYSA-N 100676-05-9 Natural products OC1C(O)C(O)C(CO)OC1OCC1C(O)C(O)C(O)C(OC2C(OC(O)C(O)C2O)CO)O1 OWEGMIWEEQEYGQ-UHFFFAOYSA-N 0.000 description 14
- GUBGYTABKSRVRQ-PICCSMPSSA-N Maltose Natural products O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@@H](CO)OC(O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-PICCSMPSSA-N 0.000 description 14
- 238000000746 purification Methods 0.000 description 14
- 208000015181 infectious disease Diseases 0.000 description 12
- 238000003860 storage Methods 0.000 description 12
- 238000010200 validation analysis Methods 0.000 description 12
- 230000006870 function Effects 0.000 description 11
- 238000004255 ion exchange chromatography Methods 0.000 description 11
- 239000012263 liquid product Substances 0.000 description 11
- 235000017281 sodium acetate Nutrition 0.000 description 11
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 10
- 230000027455 binding Effects 0.000 description 10
- 239000001632 sodium acetate Substances 0.000 description 10
- FBPFZTCFMRRESA-FSIIMWSLSA-N D-Glucitol Natural products OC[C@H](O)[C@H](O)[C@@H](O)[C@H](O)CO FBPFZTCFMRRESA-FSIIMWSLSA-N 0.000 description 9
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 9
- 239000000427 antigen Substances 0.000 description 9
- 102000036639 antigens Human genes 0.000 description 9
- 108091007433 antigens Proteins 0.000 description 9
- 238000005341 cation exchange Methods 0.000 description 9
- 238000004519 manufacturing process Methods 0.000 description 9
- 239000007974 sodium acetate buffer Substances 0.000 description 9
- 239000000600 sorbitol Substances 0.000 description 9
- 238000005194 fractionation Methods 0.000 description 8
- 230000002458 infectious effect Effects 0.000 description 8
- 239000012528 membrane Substances 0.000 description 8
- 235000010482 polyoxyethylene sorbitan monooleate Nutrition 0.000 description 8
- 229920000053 polysorbate 80 Polymers 0.000 description 8
- 239000007858 starting material Substances 0.000 description 8
- 238000012360 testing method Methods 0.000 description 8
- 208000031981 Thrombocytopenic Idiopathic Purpura Diseases 0.000 description 7
- MZVQCMJNVPIDEA-UHFFFAOYSA-N [CH2]CN(CC)CC Chemical compound [CH2]CN(CC)CC MZVQCMJNVPIDEA-UHFFFAOYSA-N 0.000 description 7
- 201000003710 autoimmune thrombocytopenic purpura Diseases 0.000 description 7
- 238000004587 chromatography analysis Methods 0.000 description 7
- 150000002632 lipids Chemical class 0.000 description 7
- 230000009467 reduction Effects 0.000 description 7
- 150000003839 salts Chemical class 0.000 description 7
- 210000002966 serum Anatomy 0.000 description 7
- 208000030939 Chronic inflammatory demyelinating polyneuropathy Diseases 0.000 description 6
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 6
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 6
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 6
- 150000001720 carbohydrates Chemical class 0.000 description 6
- 235000014633 carbohydrates Nutrition 0.000 description 6
- 201000005795 chronic inflammatory demyelinating polyneuritis Diseases 0.000 description 6
- 238000009826 distribution Methods 0.000 description 6
- 229940079593 drug Drugs 0.000 description 6
- 239000008103 glucose Substances 0.000 description 6
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 5
- 241000725303 Human immunodeficiency virus Species 0.000 description 5
- 230000008901 benefit Effects 0.000 description 5
- 238000001514 detection method Methods 0.000 description 5
- 239000006167 equilibration buffer Substances 0.000 description 5
- 239000000463 material Substances 0.000 description 5
- 229910000162 sodium phosphate Inorganic materials 0.000 description 5
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 5
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 5
- 206010067484 Adverse reaction Diseases 0.000 description 4
- 230000006838 adverse reaction Effects 0.000 description 4
- 230000015572 biosynthetic process Effects 0.000 description 4
- 210000004369 blood Anatomy 0.000 description 4
- 239000008280 blood Substances 0.000 description 4
- 239000007853 buffer solution Substances 0.000 description 4
- 238000005119 centrifugation Methods 0.000 description 4
- 230000000295 complement effect Effects 0.000 description 4
- 230000008030 elimination Effects 0.000 description 4
- 238000003379 elimination reaction Methods 0.000 description 4
- 238000011534 incubation Methods 0.000 description 4
- 238000001802 infusion Methods 0.000 description 4
- 238000005342 ion exchange Methods 0.000 description 4
- 239000011159 matrix material Substances 0.000 description 4
- 208000023275 Autoimmune disease Diseases 0.000 description 3
- 241000710780 Bovine viral diarrhea virus 1 Species 0.000 description 3
- WQZGKKKJIJFFOK-QTVWNMPRSA-N D-mannopyranose Chemical compound OC[C@H]1OC(O)[C@@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-QTVWNMPRSA-N 0.000 description 3
- 239000004471 Glycine Substances 0.000 description 3
- 241000711549 Hepacivirus C Species 0.000 description 3
- 241000709721 Hepatovirus A Species 0.000 description 3
- 108091005804 Peptidases Proteins 0.000 description 3
- 239000004365 Protease Substances 0.000 description 3
- 206010047115 Vasculitis Diseases 0.000 description 3
- 230000002378 acidificating effect Effects 0.000 description 3
- 230000002391 anti-complement effect Effects 0.000 description 3
- 108010008730 anticomplement Proteins 0.000 description 3
- GUBGYTABKSRVRQ-QUYVBRFLSA-N beta-maltose Chemical compound OC[C@H]1O[C@H](O[C@H]2[C@H](O)[C@@H](O)[C@H](O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@@H]1O GUBGYTABKSRVRQ-QUYVBRFLSA-N 0.000 description 3
- 230000002950 deficient Effects 0.000 description 3
- 239000012149 elution buffer Substances 0.000 description 3
- 238000011067 equilibration Methods 0.000 description 3
- 239000000706 filtrate Substances 0.000 description 3
- 239000000185 hemagglutinin Substances 0.000 description 3
- 230000002519 immonomodulatory effect Effects 0.000 description 3
- 238000007918 intramuscular administration Methods 0.000 description 3
- 239000003456 ion exchange resin Substances 0.000 description 3
- 229920003303 ion-exchange polymer Polymers 0.000 description 3
- 244000309711 non-enveloped viruses Species 0.000 description 3
- 230000036961 partial effect Effects 0.000 description 3
- 229920002492 poly(sulfone) Polymers 0.000 description 3
- 230000002265 prevention Effects 0.000 description 3
- 230000002829 reductive effect Effects 0.000 description 3
- 238000000926 separation method Methods 0.000 description 3
- 239000001488 sodium phosphate Substances 0.000 description 3
- 241000894006 Bacteria Species 0.000 description 2
- 102100022641 Coagulation factor IX Human genes 0.000 description 2
- 206010010356 Congenital anomaly Diseases 0.000 description 2
- FBPFZTCFMRRESA-JGWLITMVSA-N D-glucitol Chemical compound OC[C@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-JGWLITMVSA-N 0.000 description 2
- 238000002965 ELISA Methods 0.000 description 2
- 108010076282 Factor IX Proteins 0.000 description 2
- 206010072579 Granulomatosis with polyangiitis Diseases 0.000 description 2
- 101710154606 Hemagglutinin Proteins 0.000 description 2
- 208000011200 Kawasaki disease Diseases 0.000 description 2
- 102000004895 Lipoproteins Human genes 0.000 description 2
- 108090001030 Lipoproteins Proteins 0.000 description 2
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 2
- 239000004472 Lysine Substances 0.000 description 2
- 101710093908 Outer capsid protein VP4 Proteins 0.000 description 2
- 101710135467 Outer capsid protein sigma-1 Proteins 0.000 description 2
- 102000057297 Pepsin A Human genes 0.000 description 2
- 108090000284 Pepsin A Proteins 0.000 description 2
- 102000035195 Peptidases Human genes 0.000 description 2
- 206010035226 Plasma cell myeloma Diseases 0.000 description 2
- 101710176177 Protein A56 Proteins 0.000 description 2
- 206010037660 Pyrexia Diseases 0.000 description 2
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 2
- 201000009594 Systemic Scleroderma Diseases 0.000 description 2
- 206010042953 Systemic sclerosis Diseases 0.000 description 2
- 208000036142 Viral infection Diseases 0.000 description 2
- 229960000583 acetic acid Drugs 0.000 description 2
- 239000002253 acid Substances 0.000 description 2
- 150000007513 acids Chemical class 0.000 description 2
- 230000002411 adverse Effects 0.000 description 2
- 208000003455 anaphylaxis Diseases 0.000 description 2
- 239000004019 antithrombin Substances 0.000 description 2
- 230000004071 biological effect Effects 0.000 description 2
- 230000005540 biological transmission Effects 0.000 description 2
- 238000010322 bone marrow transplantation Methods 0.000 description 2
- PPBOKXIGFIBOGK-BDTUAEFFSA-N bvdv Chemical compound C([C@@H](C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)C(C)C)[C@@H](C)CC)C1=CN=CN1 PPBOKXIGFIBOGK-BDTUAEFFSA-N 0.000 description 2
- 238000006243 chemical reaction Methods 0.000 description 2
- 238000011210 chromatographic step Methods 0.000 description 2
- 230000007012 clinical effect Effects 0.000 description 2
- 230000004154 complement system Effects 0.000 description 2
- 150000001875 compounds Chemical class 0.000 description 2
- 238000011109 contamination Methods 0.000 description 2
- DDRJAANPRJIHGJ-UHFFFAOYSA-N creatinine Chemical compound CN1CC(=O)NC1=N DDRJAANPRJIHGJ-UHFFFAOYSA-N 0.000 description 2
- 238000000502 dialysis Methods 0.000 description 2
- 230000029087 digestion Effects 0.000 description 2
- 238000007865 diluting Methods 0.000 description 2
- 238000004090 dissolution Methods 0.000 description 2
- 238000000605 extraction Methods 0.000 description 2
- 229960004222 factor ix Drugs 0.000 description 2
- 239000000499 gel Substances 0.000 description 2
- 238000005227 gel permeation chromatography Methods 0.000 description 2
- 208000006454 hepatitis Diseases 0.000 description 2
- 231100000283 hepatitis Toxicity 0.000 description 2
- 238000010255 intramuscular injection Methods 0.000 description 2
- 239000007927 intramuscular injection Substances 0.000 description 2
- 238000011835 investigation Methods 0.000 description 2
- 239000000644 isotonic solution Substances 0.000 description 2
- 238000011068 loading method Methods 0.000 description 2
- 230000014759 maintenance of location Effects 0.000 description 2
- 230000004060 metabolic process Effects 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 208000001725 mucocutaneous lymph node syndrome Diseases 0.000 description 2
- 230000003204 osmotic effect Effects 0.000 description 2
- 229940111202 pepsin Drugs 0.000 description 2
- 210000001539 phagocyte Anatomy 0.000 description 2
- 208000005987 polymyositis Diseases 0.000 description 2
- 230000001681 protective effect Effects 0.000 description 2
- 230000006920 protein precipitation Effects 0.000 description 2
- 230000000717 retained effect Effects 0.000 description 2
- 239000012064 sodium phosphate buffer Substances 0.000 description 2
- 239000002594 sorbent Substances 0.000 description 2
- 238000003756 stirring Methods 0.000 description 2
- 150000005846 sugar alcohols Chemical class 0.000 description 2
- 238000002560 therapeutic procedure Methods 0.000 description 2
- 230000009385 viral infection Effects 0.000 description 2
- 239000008215 water for injection Substances 0.000 description 2
- BDKLKNJTMLIAFE-UHFFFAOYSA-N 2-(3-fluorophenyl)-1,3-oxazole-4-carbaldehyde Chemical compound FC1=CC=CC(C=2OC=C(C=O)N=2)=C1 BDKLKNJTMLIAFE-UHFFFAOYSA-N 0.000 description 1
- 125000000022 2-aminoethyl group Chemical group [H]C([*])([H])C([H])([H])N([H])[H] 0.000 description 1
- 229920000936 Agarose Polymers 0.000 description 1
- 108010068307 Alpha-Globulins Proteins 0.000 description 1
- 102000002572 Alpha-Globulins Human genes 0.000 description 1
- 206010002198 Anaphylactic reaction Diseases 0.000 description 1
- 206010002199 Anaphylactic shock Diseases 0.000 description 1
- 208000010839 B-cell chronic lymphocytic leukemia Diseases 0.000 description 1
- 102000006734 Beta-Globulins Human genes 0.000 description 1
- 108010087504 Beta-Globulins Proteins 0.000 description 1
- 206010010099 Combined immunodeficiency Diseases 0.000 description 1
- 201000003874 Common Variable Immunodeficiency Diseases 0.000 description 1
- 208000035473 Communicable disease Diseases 0.000 description 1
- 229920002307 Dextran Polymers 0.000 description 1
- 208000030453 Drug-Related Side Effects and Adverse reaction Diseases 0.000 description 1
- 206010013975 Dyspnoeas Diseases 0.000 description 1
- 108010049003 Fibrinogen Proteins 0.000 description 1
- 102000008946 Fibrinogen Human genes 0.000 description 1
- 241000533867 Fordia Species 0.000 description 1
- 206010018910 Haemolysis Diseases 0.000 description 1
- 206010019233 Headaches Diseases 0.000 description 1
- 208000035186 Hemolytic Autoimmune Anemia Diseases 0.000 description 1
- 208000032843 Hemorrhage Diseases 0.000 description 1
- HTTJABKRGRZYRN-UHFFFAOYSA-N Heparin Chemical compound OC1C(NC(=O)C)C(O)OC(COS(O)(=O)=O)C1OC1C(OS(O)(=O)=O)C(O)C(OC2C(C(OS(O)(=O)=O)C(OC3C(C(O)C(O)C(O3)C(O)=O)OS(O)(=O)=O)C(CO)O2)NS(O)(=O)=O)C(C(O)=O)O1 HTTJABKRGRZYRN-UHFFFAOYSA-N 0.000 description 1
- 108091006905 Human Serum Albumin Proteins 0.000 description 1
- 102000008100 Human Serum Albumin Human genes 0.000 description 1
- 241000713772 Human immunodeficiency virus 1 Species 0.000 description 1
- 241000713340 Human immunodeficiency virus 2 Species 0.000 description 1
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 1
- 102000009490 IgG Receptors Human genes 0.000 description 1
- 108010073807 IgG Receptors Proteins 0.000 description 1
- 206010022004 Influenza like illness Diseases 0.000 description 1
- 238000007696 Kjeldahl method Methods 0.000 description 1
- 206010067125 Liver injury Diseases 0.000 description 1
- AFVFQIVMOAPDHO-UHFFFAOYSA-M Methanesulfonate Chemical compound CS([O-])(=O)=O AFVFQIVMOAPDHO-UHFFFAOYSA-M 0.000 description 1
- 208000034578 Multiple myelomas Diseases 0.000 description 1
- 208000012902 Nervous system disease Diseases 0.000 description 1
- 206010029240 Neuritis Diseases 0.000 description 1
- 208000025966 Neurological disease Diseases 0.000 description 1
- 208000037581 Persistent Infection Diseases 0.000 description 1
- 206010035664 Pneumonia Diseases 0.000 description 1
- 206010036700 Primary immunodeficiency syndromes Diseases 0.000 description 1
- 208000035977 Rare disease Diseases 0.000 description 1
- 206010062237 Renal impairment Diseases 0.000 description 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 1
- 208000025747 Rheumatic disease Diseases 0.000 description 1
- 206010070834 Sensitisation Diseases 0.000 description 1
- 229920005654 Sephadex Polymers 0.000 description 1
- 239000012507 Sephadex™ Substances 0.000 description 1
- 241000710960 Sindbis virus Species 0.000 description 1
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 1
- 229930006000 Sucrose Natural products 0.000 description 1
- 208000004732 Systemic Vasculitis Diseases 0.000 description 1
- 238000011053 TCID50 method Methods 0.000 description 1
- 102000003929 Transaminases Human genes 0.000 description 1
- 108090000340 Transaminases Proteins 0.000 description 1
- 102000004338 Transferrin Human genes 0.000 description 1
- 108090000901 Transferrin Proteins 0.000 description 1
- 206010047700 Vomiting Diseases 0.000 description 1
- 208000006110 Wiskott-Aldrich syndrome Diseases 0.000 description 1
- 230000002159 abnormal effect Effects 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 239000012190 activator Substances 0.000 description 1
- 239000000654 additive Substances 0.000 description 1
- 239000011543 agarose gel Substances 0.000 description 1
- 230000002776 aggregation Effects 0.000 description 1
- 238000004220 aggregation Methods 0.000 description 1
- 230000000735 allogeneic effect Effects 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 238000012443 analytical study Methods 0.000 description 1
- 230000002052 anaphylactic effect Effects 0.000 description 1
- 150000001450 anions Chemical class 0.000 description 1
- 230000003171 anti-complementary effect Effects 0.000 description 1
- 230000003302 anti-idiotype Effects 0.000 description 1
- 201000000448 autoimmune hemolytic anemia Diseases 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 230000003115 biocidal effect Effects 0.000 description 1
- 230000008827 biological function Effects 0.000 description 1
- 230000000740 bleeding effect Effects 0.000 description 1
- 239000010836 blood and blood product Substances 0.000 description 1
- 229940125691 blood product Drugs 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 239000001913 cellulose Substances 0.000 description 1
- 229920002678 cellulose Polymers 0.000 description 1
- 229920002301 cellulose acetate Polymers 0.000 description 1
- 230000005796 circulatory shock Effects 0.000 description 1
- 238000004440 column chromatography Methods 0.000 description 1
- 230000000052 comparative effect Effects 0.000 description 1
- 238000012937 correction Methods 0.000 description 1
- 239000003246 corticosteroid Substances 0.000 description 1
- 229940109239 creatinine Drugs 0.000 description 1
- 230000001186 cumulative effect Effects 0.000 description 1
- 230000016396 cytokine production Effects 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 238000011033 desalting Methods 0.000 description 1
- 239000012538 diafiltration buffer Substances 0.000 description 1
- 150000002016 disaccharides Chemical class 0.000 description 1
- 230000008034 disappearance Effects 0.000 description 1
- 230000009977 dual effect Effects 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 210000003743 erythrocyte Anatomy 0.000 description 1
- 238000012869 ethanol precipitation Methods 0.000 description 1
- 229940012952 fibrinogen Drugs 0.000 description 1
- 239000012467 final product Substances 0.000 description 1
- 239000012530 fluid Substances 0.000 description 1
- 238000009472 formulation Methods 0.000 description 1
- 239000012634 fragment Substances 0.000 description 1
- 239000004023 fresh frozen plasma Substances 0.000 description 1
- 230000005714 functional activity Effects 0.000 description 1
- 229940009600 gammagard Drugs 0.000 description 1
- 230000002496 gastric effect Effects 0.000 description 1
- 239000012362 glacial acetic acid Substances 0.000 description 1
- 230000035931 haemagglutination Effects 0.000 description 1
- 231100000869 headache Toxicity 0.000 description 1
- 229960002897 heparin Drugs 0.000 description 1
- 229920000669 heparin Polymers 0.000 description 1
- 231100000234 hepatic damage Toxicity 0.000 description 1
- IXCSERBJSXMMFS-UHFFFAOYSA-N hydrogen chloride Substances Cl.Cl IXCSERBJSXMMFS-UHFFFAOYSA-N 0.000 description 1
- 230000000521 hyperimmunizing effect Effects 0.000 description 1
- 230000001077 hypotensive effect Effects 0.000 description 1
- 230000000951 immunodiffusion Effects 0.000 description 1
- 238000000760 immunoelectrophoresis Methods 0.000 description 1
- 230000007233 immunological mechanism Effects 0.000 description 1
- 230000001771 impaired effect Effects 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 206010022000 influenza Diseases 0.000 description 1
- 230000000977 initiatory effect Effects 0.000 description 1
- 238000002347 injection Methods 0.000 description 1
- 239000007924 injection Substances 0.000 description 1
- 238000001696 ion exchange chromatographie Methods 0.000 description 1
- 230000002427 irreversible effect Effects 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 210000003734 kidney Anatomy 0.000 description 1
- 238000011031 large-scale manufacturing process Methods 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 239000012669 liquid formulation Substances 0.000 description 1
- 230000008818 liver damage Effects 0.000 description 1
- 208000019423 liver disease Diseases 0.000 description 1
- 239000013541 low molecular weight contaminant Substances 0.000 description 1
- 206010025135 lupus erythematosus Diseases 0.000 description 1
- 239000008176 lyophilized powder Substances 0.000 description 1
- 125000003071 maltose group Chemical group 0.000 description 1
- 230000010534 mechanism of action Effects 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 229940126601 medicinal product Drugs 0.000 description 1
- 210000004779 membrane envelope Anatomy 0.000 description 1
- CXKWCBBOMKCUKX-UHFFFAOYSA-M methylene blue Chemical compound [Cl-].C1=CC(N(C)C)=CC2=[S+]C3=CC(N(C)C)=CC=C3N=C21 CXKWCBBOMKCUKX-UHFFFAOYSA-M 0.000 description 1
- 229960000907 methylthioninium chloride Drugs 0.000 description 1
- 230000003278 mimic effect Effects 0.000 description 1
- 150000002772 monosaccharides Chemical class 0.000 description 1
- 201000000050 myeloid neoplasm Diseases 0.000 description 1
- 238000001728 nano-filtration Methods 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 230000003472 neutralizing effect Effects 0.000 description 1
- 229940013982 octagam Drugs 0.000 description 1
- 230000001151 other effect Effects 0.000 description 1
- 239000011236 particulate material Substances 0.000 description 1
- 230000007505 plaque formation Effects 0.000 description 1
- 208000000813 polyradiculoneuropathy Diseases 0.000 description 1
- 239000011148 porous material Substances 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 208000012934 primary antiphospholipid syndrome Diseases 0.000 description 1
- 208000028529 primary immunodeficiency disease Diseases 0.000 description 1
- 238000011137 process chromatography Methods 0.000 description 1
- 230000002035 prolonged effect Effects 0.000 description 1
- 238000011321 prophylaxis Methods 0.000 description 1
- 235000004252 protein component Nutrition 0.000 description 1
- 238000001742 protein purification Methods 0.000 description 1
- 238000003908 quality control method Methods 0.000 description 1
- 125000001453 quaternary ammonium group Chemical group 0.000 description 1
- 230000009257 reactivity Effects 0.000 description 1
- 239000013558 reference substance Substances 0.000 description 1
- 230000004044 response Effects 0.000 description 1
- 230000000552 rheumatic effect Effects 0.000 description 1
- 206010039073 rheumatoid arthritis Diseases 0.000 description 1
- 238000012216 screening Methods 0.000 description 1
- 230000035945 sensitivity Effects 0.000 description 1
- 230000008313 sensitization Effects 0.000 description 1
- 239000000377 silicon dioxide Substances 0.000 description 1
- 229940087562 sodium acetate trihydrate Drugs 0.000 description 1
- 239000007790 solid phase Substances 0.000 description 1
- 239000011877 solvent mixture Substances 0.000 description 1
- 238000001179 sorption measurement Methods 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 238000010911 splenectomy Methods 0.000 description 1
- 238000013112 stability test Methods 0.000 description 1
- 230000000087 stabilizing effect Effects 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 238000011146 sterile filtration Methods 0.000 description 1
- 230000001954 sterilising effect Effects 0.000 description 1
- 238000004659 sterilization and disinfection Methods 0.000 description 1
- 238000007920 subcutaneous administration Methods 0.000 description 1
- 238000010254 subcutaneous injection Methods 0.000 description 1
- 239000007929 subcutaneous injection Substances 0.000 description 1
- 239000005720 sucrose Substances 0.000 description 1
- 239000010414 supernatant solution Substances 0.000 description 1
- 208000024891 symptom Diseases 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 229920001059 synthetic polymer Polymers 0.000 description 1
- 230000009885 systemic effect Effects 0.000 description 1
- 201000000596 systemic lupus erythematosus Diseases 0.000 description 1
- 230000003582 thrombocytopenic effect Effects 0.000 description 1
- 238000004448 titration Methods 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 239000012581 transferrin Substances 0.000 description 1
- 230000014599 transmission of virus Effects 0.000 description 1
- STCOOQWBFONSKY-UHFFFAOYSA-N tributyl phosphate Chemical compound CCCCOP(=O)(OCCCC)OCCCC STCOOQWBFONSKY-UHFFFAOYSA-N 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
- 230000007306 turnover Effects 0.000 description 1
- 241001529453 unidentified herpesvirus Species 0.000 description 1
- 208000019553 vascular disease Diseases 0.000 description 1
- 230000008673 vomiting Effects 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/06—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies from serum
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/06—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies from serum
- C07K16/065—Purification, fragmentation
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/395—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum
- A61K39/39591—Stabilisation, fragmentation
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/12—Antivirals
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Medicinal Chemistry (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Pharmacology & Pharmacy (AREA)
- Immunology (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Animal Behavior & Ethology (AREA)
- General Chemical & Material Sciences (AREA)
- Genetics & Genomics (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- Epidemiology (AREA)
- Mycology (AREA)
- Microbiology (AREA)
- Virology (AREA)
- Communicable Diseases (AREA)
- Oncology (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP98201909 | 1998-06-09 | ||
| US10205598P | 1998-09-28 | 1998-09-28 | |
| PCT/DK1999/000312 WO1999064462A1 (en) | 1998-06-09 | 1999-06-09 | Process for producing immunoglobulins for intravenous administration and other immunoglobulin products |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| SK18662000A3 SK18662000A3 (sk) | 2001-07-10 |
| SK288128B6 true SK288128B6 (sk) | 2013-10-02 |
Family
ID=26150417
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| SK1866-2000A SK288128B6 (sk) | 1998-06-09 | 1999-06-09 | Process for purifying immunoglobulin G (IgG), liquid immunoglobulin product and use thereof for the preparation of a medicament |
Country Status (22)
| Country | Link |
|---|---|
| EP (4) | EP1493751A1 (cs) |
| JP (1) | JP5478519B2 (cs) |
| KR (1) | KR100501263B1 (cs) |
| CN (1) | CN1196714C (cs) |
| AT (1) | ATE277950T1 (cs) |
| AU (1) | AU753468B2 (cs) |
| BR (1) | BR9911131A (cs) |
| CA (1) | CA2330170C (cs) |
| CZ (1) | CZ297199B6 (cs) |
| DE (1) | DE69920693T2 (cs) |
| DK (1) | DK1084147T3 (cs) |
| ES (1) | ES2229784T3 (cs) |
| HU (1) | HU228076B1 (cs) |
| ID (1) | ID27417A (cs) |
| IL (1) | IL140155A (cs) |
| NZ (1) | NZ509135A (cs) |
| PL (1) | PL196770B1 (cs) |
| PT (1) | PT1084147E (cs) |
| RU (1) | RU2197500C2 (cs) |
| SK (1) | SK288128B6 (cs) |
| TR (1) | TR200100303T2 (cs) |
| WO (1) | WO1999064462A1 (cs) |
Families Citing this family (77)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| ES2158776B1 (es) * | 1999-04-13 | 2002-03-16 | Apc Europ S A | Procedimiento para la obtencion de gammaglobulinas de origen animal y aplicaciones correspondientes. |
| AUPQ026799A0 (en) * | 1999-05-10 | 1999-06-03 | Csl Limited | Method of increasing protein stability by removing immunoglobulin aggregates |
| CA2400504A1 (en) * | 2000-03-10 | 2001-09-13 | Egil Lien | Composition for the treatment of heart failure |
| SE0001128D0 (sv) | 2000-03-30 | 2000-03-30 | Amersham Pharm Biotech Ab | A method of producing IgG |
| ES2184594B1 (es) * | 2001-01-17 | 2004-01-01 | Probitas Pharma Sa | Procedimiento para la produccion de gammaglobulina g humana inactivada de virus. |
| FR2824568B1 (fr) | 2001-05-11 | 2004-04-09 | Lab Francais Du Fractionnement | Procede de preparation de concentres d'immunoglobulines humaines a usage therapeutique |
| US20030223985A1 (en) * | 2002-05-29 | 2003-12-04 | The Lauridsen Group. Incorporated | Globulin protein to lower cholesterol in humans |
| WO2004024752A1 (ja) | 2002-09-11 | 2004-03-25 | Chugai Seiyaku Kabushiki Kaisha | タンパク質精製方法 |
| EP1614693A4 (en) * | 2003-03-31 | 2006-07-19 | Kirin Brewery | Purification of a human monoclonal antibody and human polyclonal antibody |
| EP1532983A1 (en) | 2003-11-18 | 2005-05-25 | ZLB Bioplasma AG | Immunoglobulin preparations having increased stability |
| JP2008500959A (ja) * | 2004-01-30 | 2008-01-17 | スオメン プナイネン リスティ ヴェリパルヴェル | ウイルスについて安全な免疫グロブリンの製造方法 |
| EP2532742B1 (en) | 2004-01-30 | 2018-08-08 | Shire Pharmaceuticals Ireland Limited | Recombinant arylsulfatase A for reducing galatosyl sulphatide levels in a subject |
| RU2252780C1 (ru) * | 2004-04-30 | 2005-05-27 | Аваков Анатолий Эдуардович | Способ получения иммуноглобулинового препарата |
| AU2005229674B2 (en) * | 2004-11-18 | 2010-11-04 | Kedrion Melville Inc. | Low concentration solvent/detergent process of immuneglobulin with pre-treatment |
| TWI391399B (zh) | 2005-05-25 | 2013-04-01 | Hoffmann La Roche | 測定溶離多肽之鹽濃度之方法 |
| KR101363777B1 (ko) | 2005-09-30 | 2014-02-14 | 메디뮨 리미티드 | 인터루킨―13 항체 조성물 |
| US9309316B2 (en) | 2005-12-20 | 2016-04-12 | Bristol-Myers Squibb Company | Stable subcutaneous protein formulations and uses thereof |
| FR2895263B1 (fr) | 2005-12-26 | 2008-05-30 | Lab Francais Du Fractionnement | Concentre d'immunoglobines g (lg) appauvri en anticorps anti-a et anti-b, et en igg polyreactives |
| ES2744499T3 (es) | 2006-04-04 | 2020-02-25 | Chiesi Farm Spa | Un proceso para la concentración de un polipéptido |
| RU2303995C1 (ru) * | 2006-04-28 | 2007-08-10 | Халлар Абдумуслимович Алиханов | Средство, обладающее иммунорегуляторным свойством и его применение для лечения аутоиммунных заболеваний |
| WO2008025748A1 (en) | 2006-08-28 | 2008-03-06 | Ares Trading S.A. | Process for the purification of fc-containing proteins |
| DE102007001521A1 (de) * | 2007-01-10 | 2008-07-17 | Matthias, Torsten, Dr. | Verwendung von Cohn-Oncley-Fraktionen II und II/III zur Behandlung des systemischen Lupus erythematodes |
| UA85734C2 (ru) * | 2007-02-14 | 2009-02-25 | Костянтин Васильевич Курищук | Способ инактивации вирусов при получении иммуноглобулина |
| UA85741C2 (ru) * | 2007-02-27 | 2009-02-25 | Костянтин Васильевич Курищук | Способ получения иммуноглобулина |
| RU2352358C1 (ru) * | 2007-10-04 | 2009-04-20 | Наталия Васильевна Зубкова | Способ приготовления вирусинактивированных растворов иммуноглобулинов |
| PL2215117T5 (pl) | 2007-10-30 | 2018-06-29 | Genentech, Inc. | Oczyszczanie przeciwciał za pomocą chromatografii kationowymiennej |
| US8883146B2 (en) | 2007-11-30 | 2014-11-11 | Abbvie Inc. | Protein formulations and methods of making same |
| EP2271382B1 (en) | 2008-04-15 | 2013-03-13 | Grifols Therapeutics Inc. | Two-stage ultrafiltration/diafiltration |
| RU2410395C2 (ru) * | 2008-05-04 | 2011-01-27 | Институт биохимии и физиологии растений и микроорганизмов Российской Академии наук | Способ получения моноспецифических антител к белкам растительных клеток |
| FR2939667B1 (fr) | 2008-12-17 | 2012-01-27 | Fractionnement Et Des Biotechonologies Lab Franc | Composition d'immunoglobine g comme medicament pour le traitement de l'ictere neonatal par incompatibilite foetomaternelle dans le systeme abo |
| BRPI1012082B1 (pt) | 2009-05-27 | 2022-08-16 | Takeda Pharmaceutical Company Limited | Método para preparar uma composição de igg concentrada a partir de plasma |
| EP2519537A4 (en) * | 2009-12-29 | 2013-07-10 | Reddys Lab Ltd Dr | CLEANING PROTEINS |
| JP6078344B2 (ja) | 2010-02-04 | 2017-02-08 | ツェー・エス・エル・ベーリング・アクチエンゲゼルシャフト | 免疫グロブリン製剤 |
| EP2361636A1 (en) * | 2010-02-26 | 2011-08-31 | CSL Behring AG | Immunoglobulin preparation and storage system for an immunoglobulin preparation |
| GB201006753D0 (en) | 2010-04-22 | 2010-06-09 | Biotest Ag | Process for preparing an immunolobulin composition |
| RU2467783C2 (ru) * | 2010-07-30 | 2012-11-27 | Закрытое акционерное общество "БиоХимМак СТ" | Способ хроматографического выделения иммуноглобулина |
| ES2811526T3 (es) | 2010-12-30 | 2021-03-12 | Lab Francais Du Fractionnement | Glicoles como agentes de inactivación de patógenos |
| PL2686334T5 (pl) | 2011-03-16 | 2020-10-19 | F.Hoffmann-La Roche Ag | Chromatografia jonowymienna o ulepszonej selektywności do rozdzielania monomerów, agregatów i fragmentów polipeptydowych przez modulację fazy ruchomej |
| FR2974301B1 (fr) | 2011-04-20 | 2013-08-23 | Lab Francais Du Fractionnement | Procede de preparation d'un produit plasmatique deplete en un ou plusieurs facteurs thrombogenes |
| IL212911A0 (en) * | 2011-05-16 | 2011-07-31 | Omrix Biopharmaceuticals Ltd | Immunoglobulin reduced in thrombogenic contaminants and preparation thereof |
| EP2729566B1 (en) | 2011-07-08 | 2017-03-15 | Shire Human Genetic Therapies, Inc. | Methods for purification of arylsulfatase a |
| CN103874708B (zh) * | 2011-08-26 | 2018-07-10 | 百深有限责任公司 | 用于降低血浆来源免疫球蛋白组合物的血栓栓塞可能性的方法 |
| CN102532307B (zh) * | 2012-02-22 | 2013-06-12 | 成都蓉生药业有限责任公司 | 一种制备人免疫球蛋白的方法 |
| DK3590960T3 (da) | 2012-02-29 | 2023-04-24 | Takeda Pharmaceuticals Co | Igg-stimuleret remyelinisering af perifere nerver |
| EP2822967B1 (en) | 2012-03-09 | 2019-08-07 | CSL Behring AG | Compositions comprising secretory-like immunoglobulins |
| EP2636681A1 (en) | 2012-03-09 | 2013-09-11 | CSL Behring AG | Process for enriching IgA |
| EP2636684A1 (en) | 2012-03-09 | 2013-09-11 | CSL Behring AG | Prevention of infection |
| ES2381828B1 (es) * | 2012-03-20 | 2012-11-16 | Grifols, S.A. | PROCEDIMIENTO PARA OBTENER UNA COMPOSICION DE IgG MEDIANTE TRATAMIENTO TERMICO |
| CN104507955A (zh) * | 2012-05-31 | 2015-04-08 | 新加坡科技研究局 | 采用具有多形式官能性的颗粒对免疫球蛋白g制备物的色谱纯化 |
| SG11201407801VA (en) | 2012-05-31 | 2014-12-30 | Agency Science Tech & Res | Methods for use of mixed multifunctional surfaces for reducing aggregate content in protein preparations |
| EP2682168A1 (en) | 2012-07-02 | 2014-01-08 | Millipore Corporation | Purification of biological molecules |
| AU2014205441B2 (en) | 2013-01-09 | 2019-12-12 | Takeda Pharmaceutical Company Limited | Methods for purification of arylsulfatase A |
| AU2013203043B2 (en) * | 2013-03-15 | 2016-10-06 | Takeda Pharmaceutical Company Limited | Methods to produce a human plasma-derived igg preparation enriched in brain disease-related natural iggs |
| US10464996B2 (en) | 2013-05-13 | 2019-11-05 | Momenta Pharmaceuticals, Inc. | Methods for the treatment of neurodegeneration |
| WO2015000886A1 (en) | 2013-07-01 | 2015-01-08 | Csl Behring Ag | Process |
| KR20160029840A (ko) | 2013-07-05 | 2016-03-15 | 라보라토이레 프란카이즈 듀 프락티온네먼트 에트 데스 바이오테크놀로지스 | 친화성 크로마토그래피 매트릭스 |
| US20160257754A1 (en) | 2013-10-16 | 2016-09-08 | Momenta Pharmaceuticals Inc. | Sialylated glycoproteins |
| CN103665100A (zh) * | 2014-01-03 | 2014-03-26 | 华兰生物工程重庆有限公司 | 低温乙醇提取静注人免疫球蛋白的方法 |
| US10287315B2 (en) | 2014-03-11 | 2019-05-14 | Green Cross Holdings Corporation | Method for purifying immunoglobulin |
| FR3018450B1 (fr) | 2014-03-11 | 2016-04-15 | Lab Francais Du Fractionnement | Procede de preparation de proteines plasmatiques humaines |
| US10435670B2 (en) * | 2014-04-15 | 2019-10-08 | Boehringer Ingelheim International Gmbh | Methods, apparatuses, and systems for continuously inactivating a virus during manufacture of a biological product |
| CN104004090A (zh) * | 2014-06-12 | 2014-08-27 | 新疆德源生物工程有限公司 | 一种人免疫球蛋白的制备方法 |
| CN104356231B (zh) * | 2014-11-10 | 2017-08-08 | 北海开元生物科技有限公司 | 一种有效去除人免疫球蛋白多聚体的方法 |
| US9556253B2 (en) | 2014-12-02 | 2017-01-31 | Hemarus Therapeutics Limited | Process for increased yield of immunoglobulin from human plasma |
| CN106999588A (zh) | 2014-12-03 | 2017-08-01 | 瑞士杰特贝林生物制品有限公司 | 具有增加的稳定性的包含免疫球蛋白的药物产品 |
| FR3035971A1 (fr) | 2015-05-07 | 2016-11-11 | Lab Francais Du Fractionnement | Composition enrichie en immunoglobulines polyclonales anti-a et/ou anti-b |
| KR101657690B1 (ko) * | 2015-06-05 | 2016-09-19 | 주식회사 녹십자홀딩스 | 혈장 유래 b형 간염 사람 면역글로불린 제제의 제조방법 |
| CN105950576A (zh) * | 2016-05-26 | 2016-09-21 | 成都远睿生物技术有限公司 | 一种从牛血中提取多种蛋白的方法 |
| EP3275897A1 (en) * | 2016-07-27 | 2018-01-31 | Biotest AG | Process for preparing immunoglobulin compositions |
| CN107880116B (zh) * | 2016-09-30 | 2023-02-03 | 盖立复集团公司 | 用于制备免疫球蛋白的方法 |
| FR3064484A1 (fr) | 2017-03-31 | 2018-10-05 | Laboratoire Francais Du Fractionnement Et Des Biotechnologies | Composition d'immunoglobulines utiles pour traiter des infections virales |
| FR3064486A1 (fr) | 2017-03-31 | 2018-10-05 | Laboratoire Francais Du Fractionnement Et Des Biotechnologies | Prevention d'une infection par le virus respiratoire syncytial dans les voies respiratoires superieures |
| FR3064485A1 (fr) | 2017-03-31 | 2018-10-05 | Laboratoire Francais Du Fractionnement Et Des Biotechnologies | Traitement d'une infection par le virus respiratoire syncytial |
| KR20190047376A (ko) | 2017-10-27 | 2019-05-08 | 주식회사 녹십자 | 개선된 면역글로불린의 정제방법 |
| CN109776675A (zh) * | 2017-11-10 | 2019-05-21 | 北京博莱得利生物技术有限责任公司 | 两步离子交换层析法制备犬免疫球蛋白的方法 |
| CN112574296B (zh) * | 2020-12-30 | 2023-05-19 | 中国医学科学院输血研究所 | 一种模拟IVIg的多人份混合人血浆IgG样品的分离纯化方法 |
| KR20230148961A (ko) * | 2022-04-19 | 2023-10-26 | 에스케이플라즈마 주식회사 | 면역글로불린 정제방법 |
Family Cites Families (10)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE2364792A1 (de) * | 1973-01-15 | 1974-07-18 | South African Inventions | Verfahren zum reinigen von gammaglobulin |
| US4296027A (en) * | 1977-08-31 | 1981-10-20 | The Regents Of The University Of Minnesota | Pure intravenous human and animal gamma globulins |
| US4315919A (en) | 1980-10-06 | 1982-02-16 | Edward Shanbrom | Depyrogenation process |
| US4314997A (en) | 1980-10-06 | 1982-02-09 | Edward Shanbrom | Purification of plasma protein products |
| US4764369A (en) | 1983-07-14 | 1988-08-16 | New York Blood Center Inc. | Undenatured virus-free biologically active protein derivatives |
| US4606825A (en) * | 1985-04-22 | 1986-08-19 | J. T. Baker Chemical Company | Purification of immunoglobulin G |
| NZ216094A (en) * | 1985-05-15 | 1989-06-28 | Commw Serum Lab Commission | Method for purification of an immunoglobulin |
| DE4118912C1 (cs) | 1991-06-08 | 1992-07-02 | Biotest Pharma Gmbh, 6072 Dreieich, De | |
| FR2706466B1 (fr) * | 1993-06-14 | 1995-08-25 | Aetsrn | Concentré d'immunoglobulines G à usage thérapeutique et procédé de production dudit concentré. |
| RU2094462C1 (ru) * | 1995-11-14 | 1997-10-27 | Оловникова Наталья Ивановна | Моноклональный иммуноглобулин человека класса iggi против антигена d системы резус |
-
1999
- 1999-06-09 EP EP04077620A patent/EP1493751A1/en not_active Withdrawn
- 1999-06-09 RU RU2001101454/04A patent/RU2197500C2/ru active
- 1999-06-09 ID IDW20010033A patent/ID27417A/id unknown
- 1999-06-09 CZ CZ20004534A patent/CZ297199B6/cs not_active IP Right Cessation
- 1999-06-09 EP EP10011725.8A patent/EP2270044B1/en not_active Revoked
- 1999-06-09 DK DK99955389T patent/DK1084147T3/da active
- 1999-06-09 TR TR2001/00303T patent/TR200100303T2/xx unknown
- 1999-06-09 HU HU0101988A patent/HU228076B1/hu unknown
- 1999-06-09 PT PT99955389T patent/PT1084147E/pt unknown
- 1999-06-09 CA CA2330170A patent/CA2330170C/en not_active Expired - Fee Related
- 1999-06-09 EP EP99955389A patent/EP1084147B1/en not_active Revoked
- 1999-06-09 AU AU42572/99A patent/AU753468B2/en not_active Expired
- 1999-06-09 BR BR9911131-4A patent/BR9911131A/pt not_active Application Discontinuation
- 1999-06-09 DE DE69920693T patent/DE69920693T2/de not_active Expired - Lifetime
- 1999-06-09 SK SK1866-2000A patent/SK288128B6/sk not_active IP Right Cessation
- 1999-06-09 IL IL14015599A patent/IL140155A/xx not_active IP Right Cessation
- 1999-06-09 KR KR10-2000-7014013A patent/KR100501263B1/ko not_active Expired - Fee Related
- 1999-06-09 NZ NZ509135A patent/NZ509135A/xx not_active IP Right Cessation
- 1999-06-09 WO PCT/DK1999/000312 patent/WO1999064462A1/en not_active Ceased
- 1999-06-09 CN CNB998092819A patent/CN1196714C/zh not_active Expired - Lifetime
- 1999-06-09 EP EP10184829.9A patent/EP2272870B1/en not_active Revoked
- 1999-06-09 ES ES99955389T patent/ES2229784T3/es not_active Expired - Lifetime
- 1999-06-09 AT AT99955389T patent/ATE277950T1/de active
- 1999-06-09 PL PL344671A patent/PL196770B1/pl unknown
-
2011
- 2011-01-07 JP JP2011001813A patent/JP5478519B2/ja not_active Expired - Lifetime
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| SK288128B6 (sk) | Process for purifying immunoglobulin G (IgG), liquid immunoglobulin product and use thereof for the preparation of a medicament | |
| US7138120B2 (en) | Process for producing immunoglobulins for intravenous administration and other immunoglobulin products | |
| KR101647617B1 (ko) | 혈장으로부터 IgG가 풍부한 조성물을 준비하는 방법 | |
| SK287633B6 (sk) | Spôsob výroby humánneho gamaglobulínu G a humánny gamaglobulín G s inaktivovanými vírusmi | |
| TWI579301B (zh) | 多價免疫球蛋白之濃縮物之製造方法 | |
| CN107849086A (zh) | 源自血浆的乙型肝炎人免疫球蛋白的制备方法 | |
| Buchacher et al. | Intravenous immunoglobulin G from human plasma—purification concepts and important quality criteria | |
| MXPA00012230A (en) | Process for producing immunoglobulins for intravenous administration and other immunoglobulin products | |
| HK1151045B (en) | Liquid immunoglobulin g (lgg) product | |
| HK1151044B (en) | Process for manufacturing immunoglobulins for intravenous administration and other immunoglobulin-like products | |
| WO2025068923A2 (en) | IMMUNOGLOBULIN FORMULATIONS DEPLETED IN IgA |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| PC4A | Assignment and transfer of rights |
Owner name: CSL BEHRING AG, BERNE 22, CH Free format text: FORMER OWNER: STATENS SERUM INSTITUT, COPENHAGEN S, DK Effective date: 20110111 |
|
| MK4A | Expiry of patent |
Expiry date: 20190609 |