TWI554283B - 經由熱處理獲得IgG組成物的方法 - Google Patents
經由熱處理獲得IgG組成物的方法 Download PDFInfo
- Publication number
- TWI554283B TWI554283B TW102109161A TW102109161A TWI554283B TW I554283 B TWI554283 B TW I554283B TW 102109161 A TW102109161 A TW 102109161A TW 102109161 A TW102109161 A TW 102109161A TW I554283 B TWI554283 B TW I554283B
- Authority
- TW
- Taiwan
- Prior art keywords
- solution
- igg
- diafiltration
- carried out
- concentration
- Prior art date
Links
- 238000000034 method Methods 0.000 title claims description 104
- 238000010438 heat treatment Methods 0.000 title claims description 21
- 239000000203 mixture Substances 0.000 title claims description 16
- 230000008569 process Effects 0.000 title description 21
- 239000000243 solution Substances 0.000 claims description 121
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 claims description 84
- 229920000642 polymer Polymers 0.000 claims description 71
- 102000004169 proteins and genes Human genes 0.000 claims description 47
- 108090000623 proteins and genes Proteins 0.000 claims description 47
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 claims description 44
- 239000011780 sodium chloride Substances 0.000 claims description 42
- 239000011347 resin Substances 0.000 claims description 35
- 229920005989 resin Polymers 0.000 claims description 35
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 claims description 30
- 238000011026 diafiltration Methods 0.000 claims description 23
- 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 claims description 21
- 239000000600 sorbitol Substances 0.000 claims description 21
- 238000002347 injection Methods 0.000 claims description 15
- 239000007924 injection Substances 0.000 claims description 15
- 238000011282 treatment Methods 0.000 claims description 15
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 claims description 14
- 239000001632 sodium acetate Substances 0.000 claims description 14
- 235000017281 sodium acetate Nutrition 0.000 claims description 14
- 238000001179 sorption measurement Methods 0.000 claims description 13
- 241000700605 Viruses Species 0.000 claims description 10
- 239000012528 membrane Substances 0.000 claims description 10
- 238000001556 precipitation Methods 0.000 claims description 10
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 10
- 239000003153 chemical reaction reagent Substances 0.000 claims description 9
- 230000008030 elimination Effects 0.000 claims description 9
- 238000003379 elimination reaction Methods 0.000 claims description 9
- 239000008215 water for injection Substances 0.000 claims description 9
- 239000007853 buffer solution Substances 0.000 claims description 8
- 230000002779 inactivation Effects 0.000 claims description 7
- 239000002245 particle Substances 0.000 claims description 7
- 238000012545 processing Methods 0.000 claims description 7
- 239000004793 Polystyrene Substances 0.000 claims description 6
- 239000002253 acid Substances 0.000 claims description 6
- 239000003599 detergent Substances 0.000 claims description 6
- 239000011159 matrix material Substances 0.000 claims description 6
- 238000001728 nano-filtration Methods 0.000 claims description 6
- 230000010412 perfusion Effects 0.000 claims description 6
- 229920002223 polystyrene Polymers 0.000 claims description 6
- 239000003381 stabilizer Substances 0.000 claims description 6
- 125000002091 cationic group Chemical group 0.000 claims description 5
- 238000005277 cation exchange chromatography Methods 0.000 claims description 4
- 230000006641 stabilisation Effects 0.000 claims description 4
- 238000011105 stabilization Methods 0.000 claims description 4
- 239000013020 final formulation Substances 0.000 claims description 3
- 102000057297 Pepsin A Human genes 0.000 claims description 2
- 108090000284 Pepsin A Proteins 0.000 claims description 2
- 238000002156 mixing Methods 0.000 claims description 2
- 229940111202 pepsin Drugs 0.000 claims description 2
- 229920000193 polymethacrylate Polymers 0.000 claims description 2
- 239000012267 brine Substances 0.000 claims 1
- 230000003247 decreasing effect Effects 0.000 claims 1
- 238000010828 elution Methods 0.000 claims 1
- 150000002148 esters Chemical class 0.000 claims 1
- 125000003544 oxime group Chemical group 0.000 claims 1
- HPALAKNZSZLMCH-UHFFFAOYSA-M sodium;chloride;hydrate Chemical compound O.[Na+].[Cl-] HPALAKNZSZLMCH-UHFFFAOYSA-M 0.000 claims 1
- 238000012437 strong cation exchange chromatography Methods 0.000 claims 1
- 239000012607 strong cation exchange resin Substances 0.000 claims 1
- 238000002305 strong-anion-exchange chromatography Methods 0.000 claims 1
- 229940027941 immunoglobulin g Drugs 0.000 description 126
- 239000000047 product Substances 0.000 description 40
- 238000011084 recovery Methods 0.000 description 39
- 239000000539 dimer Substances 0.000 description 26
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 21
- 238000011068 loading method Methods 0.000 description 21
- 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 20
- 230000009467 reduction Effects 0.000 description 19
- 239000000499 gel Substances 0.000 description 18
- 239000000178 monomer Substances 0.000 description 17
- 238000009928 pasteurization Methods 0.000 description 17
- 108060003951 Immunoglobulin Proteins 0.000 description 15
- 102000018358 immunoglobulin Human genes 0.000 description 15
- 239000007788 liquid Substances 0.000 description 14
- 238000000746 purification Methods 0.000 description 14
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 13
- 238000012360 testing method Methods 0.000 description 12
- 238000001990 intravenous administration Methods 0.000 description 11
- 239000002202 Polyethylene glycol Substances 0.000 description 10
- 230000000694 effects Effects 0.000 description 10
- 230000003287 optical effect Effects 0.000 description 10
- 229920001223 polyethylene glycol Polymers 0.000 description 10
- 238000004220 aggregation Methods 0.000 description 9
- 230000002776 aggregation Effects 0.000 description 9
- 238000005194 fractionation Methods 0.000 description 9
- 238000004128 high performance liquid chromatography Methods 0.000 description 9
- 150000003839 salts Chemical class 0.000 description 9
- 238000000926 separation method Methods 0.000 description 8
- 238000004587 chromatography analysis Methods 0.000 description 7
- 238000002360 preparation method Methods 0.000 description 7
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 6
- -1 cation sulfonate Chemical class 0.000 description 6
- WWZKQHOCKIZLMA-UHFFFAOYSA-N octanoic acid Chemical compound CCCCCCCC(O)=O WWZKQHOCKIZLMA-UHFFFAOYSA-N 0.000 description 6
- 239000002244 precipitate Substances 0.000 description 6
- 238000003860 storage Methods 0.000 description 6
- 239000006228 supernatant Substances 0.000 description 6
- 229940024606 amino acid Drugs 0.000 description 5
- 150000001413 amino acids Chemical class 0.000 description 5
- 229920005862 polyol Polymers 0.000 description 5
- 150000003077 polyols Chemical class 0.000 description 5
- 239000007858 starting material Substances 0.000 description 5
- 230000009424 thromboembolic effect Effects 0.000 description 5
- STCOOQWBFONSKY-UHFFFAOYSA-N tributyl phosphate Chemical compound CCCCOP(=O)(OCCCC)OCCCC STCOOQWBFONSKY-UHFFFAOYSA-N 0.000 description 5
- 102000004190 Enzymes Human genes 0.000 description 4
- 108090000790 Enzymes Proteins 0.000 description 4
- 108091005804 Peptidases Proteins 0.000 description 4
- 102000035195 Peptidases Human genes 0.000 description 4
- 229920002684 Sepharose Polymers 0.000 description 4
- 238000009826 distribution Methods 0.000 description 4
- 229940088598 enzyme Drugs 0.000 description 4
- 239000000835 fiber Substances 0.000 description 4
- 239000000706 filtrate Substances 0.000 description 4
- 239000012467 final product Substances 0.000 description 4
- 238000009472 formulation Methods 0.000 description 4
- 238000001802 infusion Methods 0.000 description 4
- 238000004519 manufacturing process Methods 0.000 description 4
- 239000000463 material Substances 0.000 description 4
- 238000006116 polymerization reaction Methods 0.000 description 4
- 239000007787 solid Substances 0.000 description 4
- 238000000108 ultra-filtration Methods 0.000 description 4
- 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 3
- 239000004471 Glycine Substances 0.000 description 3
- 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 3
- 102000013566 Plasminogen Human genes 0.000 description 3
- 108010051456 Plasminogen Proteins 0.000 description 3
- 239000004721 Polyphenylene oxide Substances 0.000 description 3
- 208000031951 Primary immunodeficiency Diseases 0.000 description 3
- 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 3
- 229930006000 Sucrose Natural products 0.000 description 3
- 229920004890 Triton X-100 Polymers 0.000 description 3
- 239000013504 Triton X-100 Substances 0.000 description 3
- 238000010521 absorption reaction Methods 0.000 description 3
- 230000002378 acidificating effect Effects 0.000 description 3
- 239000003463 adsorbent Substances 0.000 description 3
- OBETXYAYXDNJHR-UHFFFAOYSA-N alpha-ethylcaproic acid Natural products CCCCC(CC)C(O)=O OBETXYAYXDNJHR-UHFFFAOYSA-N 0.000 description 3
- 238000004458 analytical method Methods 0.000 description 3
- 238000005119 centrifugation Methods 0.000 description 3
- 230000008859 change Effects 0.000 description 3
- 239000003795 chemical substances by application Substances 0.000 description 3
- 230000001143 conditioned effect Effects 0.000 description 3
- 238000004925 denaturation Methods 0.000 description 3
- 230000036425 denaturation Effects 0.000 description 3
- 238000010790 dilution Methods 0.000 description 3
- 239000012895 dilution Substances 0.000 description 3
- 238000004090 dissolution Methods 0.000 description 3
- 238000001962 electrophoresis Methods 0.000 description 3
- 238000001914 filtration Methods 0.000 description 3
- 239000012634 fragment Substances 0.000 description 3
- 229940099472 immunoglobulin a Drugs 0.000 description 3
- 238000007918 intramuscular administration Methods 0.000 description 3
- 150000002923 oximes Chemical class 0.000 description 3
- 229920000570 polyether Polymers 0.000 description 3
- 229920002098 polyfluorene Polymers 0.000 description 3
- 239000011148 porous material Substances 0.000 description 3
- 239000003805 procoagulant Substances 0.000 description 3
- 238000007920 subcutaneous administration Methods 0.000 description 3
- 239000005720 sucrose Substances 0.000 description 3
- 235000000346 sugar Nutrition 0.000 description 3
- 150000008163 sugars Chemical class 0.000 description 3
- 239000000725 suspension Substances 0.000 description 3
- 230000001225 therapeutic effect Effects 0.000 description 3
- 108010088751 Albumins Proteins 0.000 description 2
- 102000009027 Albumins Human genes 0.000 description 2
- 108010039209 Blood Coagulation Factors Proteins 0.000 description 2
- 102000015081 Blood Coagulation Factors Human genes 0.000 description 2
- 241000711549 Hepacivirus C Species 0.000 description 2
- 241000709721 Hepatovirus A Species 0.000 description 2
- 241000725303 Human immunodeficiency virus Species 0.000 description 2
- 206010020751 Hypersensitivity Diseases 0.000 description 2
- 206010021143 Hypoxia Diseases 0.000 description 2
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 2
- 206010061598 Immunodeficiency Diseases 0.000 description 2
- 208000029462 Immunodeficiency disease Diseases 0.000 description 2
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 2
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 2
- 108090001030 Lipoproteins Proteins 0.000 description 2
- 102000004895 Lipoproteins Human genes 0.000 description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 2
- 108010094028 Prothrombin Proteins 0.000 description 2
- 102100027378 Prothrombin Human genes 0.000 description 2
- 239000003957 anion exchange resin Substances 0.000 description 2
- 230000002391 anti-complement effect Effects 0.000 description 2
- 108010008730 anticomplement Proteins 0.000 description 2
- 239000007864 aqueous solution Substances 0.000 description 2
- 230000015572 biosynthetic process Effects 0.000 description 2
- 239000008280 blood Substances 0.000 description 2
- 210000004369 blood Anatomy 0.000 description 2
- 239000003114 blood coagulation factor Substances 0.000 description 2
- 229920005549 butyl rubber Polymers 0.000 description 2
- 229920002301 cellulose acetate Polymers 0.000 description 2
- 238000004140 cleaning Methods 0.000 description 2
- 238000007796 conventional method Methods 0.000 description 2
- 230000007812 deficiency Effects 0.000 description 2
- 230000006866 deterioration Effects 0.000 description 2
- 238000011067 equilibration Methods 0.000 description 2
- 238000004817 gas chromatography Methods 0.000 description 2
- 239000011521 glass Substances 0.000 description 2
- 230000007954 hypoxia Effects 0.000 description 2
- 230000007813 immunodeficiency Effects 0.000 description 2
- 239000012535 impurity Substances 0.000 description 2
- 238000011534 incubation Methods 0.000 description 2
- 238000011835 investigation Methods 0.000 description 2
- 238000004255 ion exchange chromatography Methods 0.000 description 2
- 230000002427 irreversible effect Effects 0.000 description 2
- 230000014759 maintenance of location Effects 0.000 description 2
- 238000005259 measurement Methods 0.000 description 2
- 230000003204 osmotic effect Effects 0.000 description 2
- 238000005325 percolation Methods 0.000 description 2
- 239000000546 pharmaceutical excipient Substances 0.000 description 2
- 238000011085 pressure filtration Methods 0.000 description 2
- 229940117323 privigen Drugs 0.000 description 2
- 230000000328 pro-aggregatory effect Effects 0.000 description 2
- 230000002797 proteolythic effect Effects 0.000 description 2
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 2
- 229940039716 prothrombin Drugs 0.000 description 2
- 239000013049 sediment Substances 0.000 description 2
- 229910052708 sodium Inorganic materials 0.000 description 2
- 239000011734 sodium Substances 0.000 description 2
- 230000000007 visual effect Effects 0.000 description 2
- 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 description 1
- 208000029483 Acquired immunodeficiency Diseases 0.000 description 1
- 239000004925 Acrylic resin Substances 0.000 description 1
- 229920000178 Acrylic resin Polymers 0.000 description 1
- 229920001817 Agar Polymers 0.000 description 1
- 208000023275 Autoimmune disease Diseases 0.000 description 1
- 208000010839 B-cell chronic lymphocytic leukemia Diseases 0.000 description 1
- LSNNMFCWUKXFEE-UHFFFAOYSA-M Bisulfite Chemical compound OS([O-])=O LSNNMFCWUKXFEE-UHFFFAOYSA-M 0.000 description 1
- 239000004215 Carbon black (E152) Substances 0.000 description 1
- KRKNYBCHXYNGOX-UHFFFAOYSA-K Citrate Chemical compound [O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O KRKNYBCHXYNGOX-UHFFFAOYSA-K 0.000 description 1
- 206010010356 Congenital anomaly Diseases 0.000 description 1
- 206010011831 Cytomegalovirus infection Diseases 0.000 description 1
- 229920002271 DEAE-Sepharose Polymers 0.000 description 1
- 241000991587 Enterovirus C Species 0.000 description 1
- VGGSQFUCUMXWEO-UHFFFAOYSA-N Ethene Chemical compound C=C VGGSQFUCUMXWEO-UHFFFAOYSA-N 0.000 description 1
- 239000005977 Ethylene Substances 0.000 description 1
- 108010074864 Factor XI Proteins 0.000 description 1
- 108010071241 Factor XIIa Proteins 0.000 description 1
- 108010080805 Factor XIa Proteins 0.000 description 1
- 108010088842 Fibrinolysin Proteins 0.000 description 1
- 102000006395 Globulins Human genes 0.000 description 1
- 108010044091 Globulins Proteins 0.000 description 1
- 208000031886 HIV Infections Diseases 0.000 description 1
- 208000037357 HIV infectious disease Diseases 0.000 description 1
- 241000700721 Hepatitis B virus Species 0.000 description 1
- 208000007514 Herpes zoster Diseases 0.000 description 1
- 102000018071 Immunoglobulin Fc Fragments Human genes 0.000 description 1
- 108010091135 Immunoglobulin Fc Fragments Proteins 0.000 description 1
- 108060005987 Kallikrein Proteins 0.000 description 1
- 102000001399 Kallikrein Human genes 0.000 description 1
- 208000011200 Kawasaki disease Diseases 0.000 description 1
- 108010077861 Kininogens Proteins 0.000 description 1
- 102000010631 Kininogens Human genes 0.000 description 1
- 102000002397 Kinins Human genes 0.000 description 1
- 108010093008 Kinins Proteins 0.000 description 1
- 108090001090 Lectins Proteins 0.000 description 1
- 102000004856 Lectins Human genes 0.000 description 1
- 208000031422 Lymphocytic Chronic B-Cell Leukemia Diseases 0.000 description 1
- 241000702321 Microvirus Species 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 239000002033 PVDF binder Substances 0.000 description 1
- 108090000113 Plasma Kallikrein Proteins 0.000 description 1
- 102000003827 Plasma Kallikrein Human genes 0.000 description 1
- 239000004698 Polyethylene Substances 0.000 description 1
- 229920000265 Polyparaphenylene Polymers 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 206010037549 Purpura Diseases 0.000 description 1
- 241001672981 Purpura Species 0.000 description 1
- 208000001647 Renal Insufficiency Diseases 0.000 description 1
- 206010054979 Secondary immunodeficiency Diseases 0.000 description 1
- 229920002472 Starch Polymers 0.000 description 1
- 108090000190 Thrombin Proteins 0.000 description 1
- 229920004897 Triton X-45 Polymers 0.000 description 1
- 238000010306 acid treatment Methods 0.000 description 1
- NIXOWILDQLNWCW-UHFFFAOYSA-N acrylic acid group Chemical group C(C=C)(=O)O NIXOWILDQLNWCW-UHFFFAOYSA-N 0.000 description 1
- 239000012190 activator Substances 0.000 description 1
- 206010000891 acute myocardial infarction Diseases 0.000 description 1
- 239000008272 agar Substances 0.000 description 1
- 208000026935 allergic disease Diseases 0.000 description 1
- 230000007815 allergy Effects 0.000 description 1
- 229910000147 aluminium phosphate Inorganic materials 0.000 description 1
- 238000012801 analytical assay Methods 0.000 description 1
- 238000005571 anion exchange chromatography Methods 0.000 description 1
- 125000000129 anionic group Chemical group 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- 239000000440 bentonite Substances 0.000 description 1
- 229910000278 bentonite Inorganic materials 0.000 description 1
- SVPXDRXYRYOSEX-UHFFFAOYSA-N bentoquatam Chemical compound O.O=[Si]=O.O=[Al]O[Al]=O SVPXDRXYRYOSEX-UHFFFAOYSA-N 0.000 description 1
- 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 1
- 229960000074 biopharmaceutical Drugs 0.000 description 1
- 238000010322 bone marrow transplantation Methods 0.000 description 1
- 239000000872 buffer Substances 0.000 description 1
- 150000001720 carbohydrates Chemical class 0.000 description 1
- 235000014633 carbohydrates Nutrition 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 239000003729 cation exchange resin Substances 0.000 description 1
- 239000001913 cellulose Substances 0.000 description 1
- 229920002678 cellulose Polymers 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 238000013375 chromatographic separation Methods 0.000 description 1
- 239000003593 chromogenic compound Substances 0.000 description 1
- 208000032852 chronic lymphocytic leukemia Diseases 0.000 description 1
- 238000005253 cladding Methods 0.000 description 1
- 238000000975 co-precipitation Methods 0.000 description 1
- 230000000295 complement effect Effects 0.000 description 1
- 239000012141 concentrate Substances 0.000 description 1
- 239000000356 contaminant Substances 0.000 description 1
- 238000011109 contamination Methods 0.000 description 1
- 238000012258 culturing Methods 0.000 description 1
- 230000001351 cycling effect Effects 0.000 description 1
- 230000001086 cytosolic effect Effects 0.000 description 1
- 230000009849 deactivation Effects 0.000 description 1
- 238000000354 decomposition reaction Methods 0.000 description 1
- 230000007423 decrease Effects 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 238000007865 diluting Methods 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- BNIILDVGGAEEIG-UHFFFAOYSA-L disodium hydrogen phosphate Chemical compound [Na+].[Na+].OP([O-])([O-])=O BNIILDVGGAEEIG-UHFFFAOYSA-L 0.000 description 1
- 229910000397 disodium phosphate Inorganic materials 0.000 description 1
- 235000019800 disodium phosphate Nutrition 0.000 description 1
- 238000010494 dissociation reaction Methods 0.000 description 1
- 230000005593 dissociations Effects 0.000 description 1
- 230000010102 embolization Effects 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 229940028757 flebogamma Drugs 0.000 description 1
- 238000013467 fragmentation Methods 0.000 description 1
- 238000006062 fragmentation reaction Methods 0.000 description 1
- 229940069042 gamunex Drugs 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 229920006158 high molecular weight polymer Polymers 0.000 description 1
- 239000012510 hollow fiber Substances 0.000 description 1
- 208000033519 human immunodeficiency virus infectious disease Diseases 0.000 description 1
- 229930195733 hydrocarbon Natural products 0.000 description 1
- 150000002430 hydrocarbons Chemical class 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 238000009177 immunoglobulin therapy Methods 0.000 description 1
- 229940072221 immunoglobulins Drugs 0.000 description 1
- 208000015181 infectious disease Diseases 0.000 description 1
- 230000002757 inflammatory effect Effects 0.000 description 1
- 229940008228 intravenous immunoglobulins Drugs 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 201000006370 kidney failure Diseases 0.000 description 1
- 238000011031 large-scale manufacturing process Methods 0.000 description 1
- 239000002523 lectin Substances 0.000 description 1
- 239000012669 liquid formulation Substances 0.000 description 1
- 239000012263 liquid product Substances 0.000 description 1
- 239000006193 liquid solution Substances 0.000 description 1
- 206010025135 lupus erythematosus Diseases 0.000 description 1
- 210000004779 membrane envelope Anatomy 0.000 description 1
- 238000001471 micro-filtration Methods 0.000 description 1
- 208000001725 mucocutaneous lymph node syndrome Diseases 0.000 description 1
- 108091005763 multidomain proteins Proteins 0.000 description 1
- 201000001119 neuropathy Diseases 0.000 description 1
- 230000007823 neuropathy Effects 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
- 230000014207 opsonization Effects 0.000 description 1
- 239000003960 organic solvent Substances 0.000 description 1
- 238000010979 pH adjustment Methods 0.000 description 1
- 244000052769 pathogen Species 0.000 description 1
- 230000001717 pathogenic effect Effects 0.000 description 1
- 208000033808 peripheral neuropathy Diseases 0.000 description 1
- 239000010451 perlite Substances 0.000 description 1
- 235000019362 perlite Nutrition 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 230000000704 physical effect Effects 0.000 description 1
- 229940012957 plasmin Drugs 0.000 description 1
- 229920001983 poloxamer Polymers 0.000 description 1
- 229920000573 polyethylene Polymers 0.000 description 1
- 238000000710 polymer precipitation Methods 0.000 description 1
- 229920000136 polysorbate Polymers 0.000 description 1
- 229920002981 polyvinylidene fluoride Polymers 0.000 description 1
- 230000001376 precipitating effect Effects 0.000 description 1
- 238000004321 preservation Methods 0.000 description 1
- 230000002265 prevention Effects 0.000 description 1
- 238000011027 product recovery Methods 0.000 description 1
- 230000002035 prolonged effect Effects 0.000 description 1
- 230000001737 promoting effect Effects 0.000 description 1
- 239000003223 protective agent Substances 0.000 description 1
- 238000000275 quality assurance Methods 0.000 description 1
- 238000003908 quality control method Methods 0.000 description 1
- 239000004627 regenerated cellulose Substances 0.000 description 1
- 230000004044 response Effects 0.000 description 1
- 238000012552 review Methods 0.000 description 1
- 239000012266 salt solution Substances 0.000 description 1
- 238000005070 sampling Methods 0.000 description 1
- 238000004062 sedimentation Methods 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- 239000007974 sodium acetate buffer Substances 0.000 description 1
- 239000001488 sodium phosphate Substances 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 239000006076 specific stabilizer Substances 0.000 description 1
- 235000019698 starch Nutrition 0.000 description 1
- 239000008107 starch Substances 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 238000012799 strong cation exchange Methods 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 125000000472 sulfonyl group Chemical group *S(*)(=O)=O 0.000 description 1
- 239000013589 supplement Substances 0.000 description 1
- 208000011580 syndromic disease Diseases 0.000 description 1
- 239000000057 synthetic resin Substances 0.000 description 1
- 229920003002 synthetic resin Polymers 0.000 description 1
- 229960004072 thrombin Drugs 0.000 description 1
- 230000000699 topical effect Effects 0.000 description 1
- GPRLSGONYQIRFK-MNYXATJNSA-N triton Chemical compound [3H+] GPRLSGONYQIRFK-MNYXATJNSA-N 0.000 description 1
- 229960004295 valine Drugs 0.000 description 1
- 230000003612 virological effect Effects 0.000 description 1
- 238000011179 visual inspection Methods 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/14—Extraction; Separation; Purification
- C07K1/36—Extraction; Separation; Purification by a combination of two or more processes of different types
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/14—Extraction; Separation; Purification
- C07K1/16—Extraction; Separation; Purification by chromatography
- C07K1/18—Ion-exchange chromatography
-
- 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
- A61K39/39516—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum from serum, plasma
- A61K39/39525—Purification
-
- 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
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
- A61P37/06—Immunosuppressants, e.g. drugs for graft rejection
-
- 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
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/21—Immunoglobulins specific features characterized by taxonomic origin from primates, e.g. man
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Immunology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Engineering & Computer Science (AREA)
- Analytical Chemistry (AREA)
- Veterinary Medicine (AREA)
- Animal Behavior & Ethology (AREA)
- Pharmacology & Pharmacy (AREA)
- Public Health (AREA)
- Microbiology (AREA)
- Epidemiology (AREA)
- Mycology (AREA)
- General Chemical & Material Sciences (AREA)
- Transplantation (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Confectionery (AREA)
- Acyclic And Carbocyclic Compounds In Medicinal Compositions (AREA)
- Medicinal Preparation (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| ES201230413A ES2381828B1 (es) | 2012-03-20 | 2012-03-20 | PROCEDIMIENTO PARA OBTENER UNA COMPOSICION DE IgG MEDIANTE TRATAMIENTO TERMICO |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| TW201343179A TW201343179A (zh) | 2013-11-01 |
| TWI554283B true TWI554283B (zh) | 2016-10-21 |
Family
ID=46053016
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| TW102109161A TWI554283B (zh) | 2012-03-20 | 2013-03-15 | 經由熱處理獲得IgG組成物的方法 |
Country Status (21)
| Country | Link |
|---|---|
| US (1) | US9200032B2 (enExample) |
| EP (1) | EP2641912B1 (enExample) |
| JP (2) | JP6048936B2 (enExample) |
| KR (1) | KR101840064B1 (enExample) |
| CN (1) | CN103319592B (enExample) |
| AR (1) | AR090337A1 (enExample) |
| AU (1) | AU2013201853B2 (enExample) |
| BR (1) | BR102013006411A2 (enExample) |
| CA (1) | CA2809513C (enExample) |
| CL (1) | CL2013000688A1 (enExample) |
| ES (2) | ES2381828B1 (enExample) |
| HU (1) | HUE027915T2 (enExample) |
| IL (1) | IL225197A (enExample) |
| MX (1) | MX339268B (enExample) |
| MY (1) | MY165024A (enExample) |
| PL (1) | PL2641912T3 (enExample) |
| PT (1) | PT2641912T (enExample) |
| RU (1) | RU2636049C2 (enExample) |
| SG (1) | SG193738A1 (enExample) |
| TW (1) | TWI554283B (enExample) |
| UY (1) | UY34679A (enExample) |
Families Citing this family (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP2990033A1 (fr) * | 2014-08-26 | 2016-03-02 | Carlina Technologies | Procédé de préparation de nanoprécipites de peptide ou protéine de faible poids moléculaire |
| HUE042984T2 (hu) * | 2015-08-31 | 2019-07-29 | Inst Grifols S A | Eljárás immunglobulinok elõállítására |
| RU2708394C2 (ru) * | 2016-09-26 | 2019-12-06 | Институто Грифольс,С.А. | Способ получения иммуноглобулинов |
| IL277797B1 (en) * | 2018-04-12 | 2024-11-01 | Amgen Inc | Methods for making stable protein compositions |
| CN112557643B (zh) * | 2019-09-26 | 2023-04-14 | 菲鹏生物股份有限公司 | 变性IgG和类风湿因子免疫抗原及制备方法 |
| CN112858671B (zh) * | 2019-11-27 | 2022-12-27 | 菲鹏生物股份有限公司 | 制备类风湿因子检测试剂的方法、类风湿因子检测试剂、试剂盒和检测方法 |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN1311797A (zh) * | 1998-06-09 | 2001-09-05 | 斯塔滕斯血清研究所 | 生产用于静脉给药的免疫球蛋白和其他免疫球蛋白产品的方法 |
| CN101679509A (zh) * | 2007-06-01 | 2010-03-24 | 弗·哈夫曼-拉罗切有限公司 | 免疫球蛋白纯化 |
Family Cites Families (21)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US514375A (en) | 1894-02-06 | miller | ||
| CA1064396A (en) | 1975-02-18 | 1979-10-16 | Myer L. Coval | Fractional precipitation of gamma globulin with polyethylene glycol |
| US4165370A (en) | 1976-05-21 | 1979-08-21 | Coval M L | Injectable gamma globulin |
| EP0035204B2 (en) | 1980-03-05 | 1991-05-22 | Miles Inc. | Pasteurized therapeutically active protein compositions |
| US4396608A (en) | 1981-08-24 | 1983-08-02 | Cutter Laboratories | Intravenously injectable immune serum globulin |
| ES506679A0 (es) | 1981-10-29 | 1982-08-16 | Green Cross Corp | Un procedimiento para preparar una immunoglobulina adecuada para inyeccion intravenosa |
| US4540573A (en) | 1983-07-14 | 1985-09-10 | New York Blood Center, Inc. | Undenatured virus-free biologically active protein derivatives |
| JPH0825902B2 (ja) | 1985-02-21 | 1996-03-13 | 株式会社ミドリ十字 | γ−グロブリンの加熱処理方法 |
| JPH0662436B2 (ja) | 1986-05-19 | 1994-08-17 | 株式会社ミドリ十字 | 静注用免疫グロブリン製剤の製造方法 |
| CA1310267C (en) | 1986-07-09 | 1992-11-17 | Yutaka Hirao | Process for heat treating chemically unmodified _-globulin |
| JP2547556B2 (ja) | 1987-02-06 | 1996-10-23 | 株式会社 ミドリ十字 | r−グロブリンの液状製剤 |
| US4876241A (en) * | 1987-05-22 | 1989-10-24 | Armour Pharmaceutical Company | Stabilization of biological and pharmaceutical products during thermal inactivation of viral and bacterial contaminants |
| ES2091161B1 (es) * | 1995-04-12 | 1997-05-16 | Grifols Grupo Sa | Procedimiento para la produccion de gammaglobulina intramuscular inactivada por pasteurizacion. |
| AT403989B (de) * | 1996-09-16 | 1998-07-27 | Immuno Ag | Verfahren zur herstellung eines plasmaprotein-hältigen arzneimittels |
| US5886154A (en) | 1997-06-20 | 1999-03-23 | Lebing; Wytold R. | Chromatographic method for high yield purification and viral inactivation of antibodies |
| UA64742C2 (uk) * | 1997-12-24 | 2004-03-15 | Альфа Терапевтик Корпорейшн | СПОСІБ ОДЕРЖАННЯ РОЗЧИНУ <font face="Symbol">g</font>-ГЛОБУЛІНУ, ПРИЗНАЧЕНОГО ДЛЯ ВНУТРІШНЬОВЕННОГО ВВЕДЕННЯ, І ПРОДУКТ, ЩО ОДЕРЖУЄТЬСЯ У ЦЕЙ СПОСІБ (ВАРІАНТИ) |
| US6281336B1 (en) * | 1998-06-09 | 2001-08-28 | Statens Serum Institut | Process for producing immunoglobulins for intravenous administration and other immunoglobulin products |
| CN1137727C (zh) * | 1998-06-25 | 2004-02-11 | 四川远大蜀阳药业有限公司 | 无保护剂双重病毒灭活制备静注免疫球蛋白工艺 |
| ES2184594B1 (es) * | 2001-01-17 | 2004-01-01 | Probitas Pharma Sa | Procedimiento para la produccion de gammaglobulina g humana inactivada de virus. |
| US7378123B2 (en) * | 2004-05-07 | 2008-05-27 | Wisconsin Alumni Research | Methods involving whey protein isolates |
| US8796430B2 (en) * | 2010-05-26 | 2014-08-05 | Baxter International Inc. | Method to produce an immunoglobulin preparation with improved yield |
-
2012
- 2012-03-20 ES ES201230413A patent/ES2381828B1/es not_active Expired - Fee Related
-
2013
- 2013-03-11 PL PL13158552.3T patent/PL2641912T3/pl unknown
- 2013-03-11 HU HUE13158552A patent/HUE027915T2/en unknown
- 2013-03-11 ES ES13158552.3T patent/ES2590045T3/es active Active
- 2013-03-11 EP EP13158552.3A patent/EP2641912B1/en active Active
- 2013-03-11 PT PT131585523T patent/PT2641912T/pt unknown
- 2013-03-13 CL CL2013000688A patent/CL2013000688A1/es unknown
- 2013-03-13 IL IL225197A patent/IL225197A/en active IP Right Grant
- 2013-03-14 CA CA2809513A patent/CA2809513C/en active Active
- 2013-03-14 MX MX2013002910A patent/MX339268B/es active IP Right Grant
- 2013-03-14 AR ARP130100825A patent/AR090337A1/es unknown
- 2013-03-15 UY UY0001034679A patent/UY34679A/es not_active Application Discontinuation
- 2013-03-15 TW TW102109161A patent/TWI554283B/zh not_active IP Right Cessation
- 2013-03-15 US US13/838,424 patent/US9200032B2/en active Active
- 2013-03-18 BR BRBR102013006411-4A patent/BR102013006411A2/pt not_active Application Discontinuation
- 2013-03-18 MY MYPI2013700437A patent/MY165024A/en unknown
- 2013-03-19 RU RU2013112276A patent/RU2636049C2/ru not_active IP Right Cessation
- 2013-03-19 AU AU2013201853A patent/AU2013201853B2/en active Active
- 2013-03-19 JP JP2013056191A patent/JP6048936B2/ja active Active
- 2013-03-19 SG SG2013020169A patent/SG193738A1/en unknown
- 2013-03-20 KR KR1020130029551A patent/KR101840064B1/ko not_active Expired - Fee Related
- 2013-03-20 CN CN201310090730.0A patent/CN103319592B/zh active Active
-
2016
- 2016-08-18 JP JP2016160479A patent/JP2016199586A/ja active Pending
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN1311797A (zh) * | 1998-06-09 | 2001-09-05 | 斯塔滕斯血清研究所 | 生产用于静脉给药的免疫球蛋白和其他免疫球蛋白产品的方法 |
| CN101679509A (zh) * | 2007-06-01 | 2010-03-24 | 弗·哈夫曼-拉罗切有限公司 | 免疫球蛋白纯化 |
Non-Patent Citations (1)
| Title |
|---|
| 2010年,Aghaie, A., et al.," Preparation, Purification and Virus Inactivation of Intravenous Immunoglobulin from Human Plasma", Hum. Antibodies, 2010, Vol.19, No.1, P.1-6. * |
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| ES2229784T3 (es) | Proceso de produccion de inmunoglobulinas para administracion intravenosa y otros productos de inmunoglobulina. | |
| ES2527915T3 (es) | Producto de inmunoglobulina G (IgG) líquido | |
| TWI554283B (zh) | 經由熱處理獲得IgG組成物的方法 | |
| ES2785375T3 (es) | Procedimiento de purificación de inmunoglobulina | |
| CA2800155A1 (en) | Method for preparing an enriched igg composition from plasma | |
| SK582002A3 (en) | Process for the production of human gammaglobulin g and virus-inactivated human gammaglobulin g | |
| JP6132839B2 (ja) | 多価免疫グロブリン濃縮物の製造方法 | |
| US20180305401A1 (en) | Processes for purifying proteins from plasma | |
| TWI526214B (zh) | 缺乏一種以上致血栓因子的血漿製品之製備方法 | |
| HK1185625B (en) | Process for obtaining an igg composition through heat treatment | |
| WO2025068923A2 (en) | IMMUNOGLOBULIN FORMULATIONS DEPLETED IN IgA | |
| KR102372105B1 (ko) | 면역글로블린의 제조방법 | |
| JP2018052822A (ja) | 免疫グロブリンの調製方法 | |
| BR102016022107B1 (pt) | Processo para preparação de uma solução de imunoglobulinas |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| MM4A | Annulment or lapse of patent due to non-payment of fees |