JP2644946B2 - ＩｇＧ− モノクロナール抗体の精製方法及びその使用方法 - Google Patents
ＩｇＧ− モノクロナール抗体の精製方法及びその使用方法Info
- Publication number
- JP2644946B2 JP2644946B2 JP4145807A JP14580792A JP2644946B2 JP 2644946 B2 JP2644946 B2 JP 2644946B2 JP 4145807 A JP4145807 A JP 4145807A JP 14580792 A JP14580792 A JP 14580792A JP 2644946 B2 JP2644946 B2 JP 2644946B2
- Authority
- JP
- Japan
- Prior art keywords
- igg
- monoclonal antibody
- antibody
- solution
- chromatographed
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Expired - Fee Related
Links
- 238000000034 method Methods 0.000 title claims abstract description 43
- 238000000746 purification Methods 0.000 title description 14
- 150000001450 anions Chemical class 0.000 claims abstract description 17
- 230000002209 hydrophobic effect Effects 0.000 claims abstract description 14
- 150000001768 cations Chemical class 0.000 claims abstract description 13
- 238000004659 sterilization and disinfection Methods 0.000 claims abstract description 11
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 claims description 34
- 239000011780 sodium chloride Substances 0.000 claims description 18
- 238000004587 chromatography analysis Methods 0.000 claims description 13
- 210000004408 hybridoma Anatomy 0.000 claims description 10
- 230000001954 sterilising effect Effects 0.000 claims description 10
- 238000010828 elution Methods 0.000 claims description 9
- 229920002684 Sepharose Polymers 0.000 claims description 6
- 238000013375 chromatographic separation Methods 0.000 claims description 5
- 239000000463 material Substances 0.000 claims description 5
- 229920000136 polysorbate Polymers 0.000 claims description 5
- 239000012228 culture supernatant Substances 0.000 claims description 4
- 238000004128 high performance liquid chromatography Methods 0.000 claims description 4
- 239000012614 Q-Sepharose Substances 0.000 claims description 3
- VEZXCJBBBCKRPI-UHFFFAOYSA-N beta-propiolactone Chemical compound O=C1CCO1 VEZXCJBBBCKRPI-UHFFFAOYSA-N 0.000 claims description 3
- 238000004519 manufacturing process Methods 0.000 claims description 3
- 235000010482 polyoxyethylene sorbitan monooleate Nutrition 0.000 claims description 3
- 229920000053 polysorbate 80 Polymers 0.000 claims description 3
- 229960000380 propiolactone Drugs 0.000 claims description 3
- 239000007858 starting material Substances 0.000 claims description 3
- 238000009281 ultraviolet germicidal irradiation Methods 0.000 claims description 3
- 239000012619 Butyl Sepharose® Substances 0.000 claims description 2
- 241001465754 Metazoa Species 0.000 claims description 2
- STCOOQWBFONSKY-UHFFFAOYSA-N tributyl phosphate Chemical compound CCCCOP(=O)(OCCCC)OCCCC STCOOQWBFONSKY-UHFFFAOYSA-N 0.000 claims 4
- 150000001875 compounds Chemical class 0.000 claims 2
- 238000011210 chromatographic step Methods 0.000 abstract description 12
- 238000009169 immunotherapy Methods 0.000 abstract description 4
- 239000000243 solution Substances 0.000 description 32
- 241000700605 Viruses Species 0.000 description 15
- 102000004169 proteins and genes Human genes 0.000 description 14
- 108090000623 proteins and genes Proteins 0.000 description 14
- 239000000872 buffer Substances 0.000 description 13
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 12
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 10
- 239000001632 sodium acetate Substances 0.000 description 10
- 235000017281 sodium acetate Nutrition 0.000 description 10
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 8
- 239000007983 Tris buffer Substances 0.000 description 8
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 6
- 230000004071 biological effect Effects 0.000 description 6
- 238000012360 testing method Methods 0.000 description 6
- 238000006243 chemical reaction Methods 0.000 description 5
- 238000011026 diafiltration Methods 0.000 description 5
- 239000000047 product Substances 0.000 description 5
- 239000007787 solid Substances 0.000 description 5
- 206010003445 Ascites Diseases 0.000 description 4
- 239000004471 Glycine Substances 0.000 description 4
- 238000001990 intravenous administration Methods 0.000 description 4
- 150000003839 salts Chemical class 0.000 description 4
- 101800000263 Acidic protein Proteins 0.000 description 3
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 3
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 3
- 235000011130 ammonium sulphate Nutrition 0.000 description 3
- 239000000499 gel Substances 0.000 description 3
- 230000002779 inactivation Effects 0.000 description 3
- 239000000203 mixture Substances 0.000 description 3
- 238000011146 sterile filtration Methods 0.000 description 3
- 238000011993 High Performance Size Exclusion Chromatography Methods 0.000 description 2
- 206010028980 Neoplasm Diseases 0.000 description 2
- 229910000831 Steel Inorganic materials 0.000 description 2
- 102000004338 Transferrin Human genes 0.000 description 2
- 108090000901 Transferrin Proteins 0.000 description 2
- 230000002159 abnormal effect Effects 0.000 description 2
- 238000005571 anion exchange chromatography Methods 0.000 description 2
- 239000007853 buffer solution Substances 0.000 description 2
- 239000008366 buffered solution Substances 0.000 description 2
- 239000012141 concentrate Substances 0.000 description 2
- 239000003814 drug Substances 0.000 description 2
- 239000012149 elution buffer Substances 0.000 description 2
- 230000007717 exclusion Effects 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 239000012530 fluid Substances 0.000 description 2
- 238000002523 gelfiltration Methods 0.000 description 2
- 239000003102 growth factor Substances 0.000 description 2
- 239000012535 impurity Substances 0.000 description 2
- 238000000338 in vitro Methods 0.000 description 2
- 238000001727 in vivo Methods 0.000 description 2
- 150000002632 lipids Chemical class 0.000 description 2
- 239000002609 medium Substances 0.000 description 2
- 239000012528 membrane Substances 0.000 description 2
- 238000012545 processing Methods 0.000 description 2
- 239000010959 steel Substances 0.000 description 2
- 238000003756 stirring Methods 0.000 description 2
- 229940124597 therapeutic agent Drugs 0.000 description 2
- 230000001225 therapeutic effect Effects 0.000 description 2
- 231100000419 toxicity Toxicity 0.000 description 2
- 230000001988 toxicity Effects 0.000 description 2
- 239000012581 transferrin Substances 0.000 description 2
- 238000005406 washing Methods 0.000 description 2
- 102000009027 Albumins Human genes 0.000 description 1
- 108010088751 Albumins Proteins 0.000 description 1
- 241000450599 DNA viruses Species 0.000 description 1
- 101000760085 Daucus carota 21 kDa protein Proteins 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 101001076408 Homo sapiens Interleukin-6 Proteins 0.000 description 1
- 101000766306 Homo sapiens Serotransferrin Proteins 0.000 description 1
- 102000010789 Interleukin-2 Receptors Human genes 0.000 description 1
- 108010038453 Interleukin-2 Receptors Proteins 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 101710093543 Probable non-specific lipid-transfer protein Proteins 0.000 description 1
- 241000702263 Reovirus sp. Species 0.000 description 1
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 1
- 108010088160 Staphylococcal Protein A Proteins 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 150000001413 amino acids Chemical class 0.000 description 1
- 239000001166 ammonium sulphate Substances 0.000 description 1
- 238000012435 analytical chromatography Methods 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 238000005277 cation exchange chromatography Methods 0.000 description 1
- 230000010261 cell growth Effects 0.000 description 1
- 238000011097 chromatography purification Methods 0.000 description 1
- 238000010961 commercial manufacture process Methods 0.000 description 1
- 239000000356 contaminant Substances 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 238000012937 correction Methods 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- ZPWVASYFFYYZEW-UHFFFAOYSA-L dipotassium hydrogen phosphate Chemical compound [K+].[K+].OP([O-])([O-])=O ZPWVASYFFYYZEW-UHFFFAOYSA-L 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 229940088598 enzyme Drugs 0.000 description 1
- 239000012467 final product Substances 0.000 description 1
- 238000009472 formulation Methods 0.000 description 1
- 230000012010 growth Effects 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 208000006454 hepatitis Diseases 0.000 description 1
- 231100000283 hepatitis Toxicity 0.000 description 1
- 229940116886 human interleukin-6 Drugs 0.000 description 1
- 244000052637 human pathogen Species 0.000 description 1
- 229910052588 hydroxylapatite Inorganic materials 0.000 description 1
- 230000000937 inactivator Effects 0.000 description 1
- 230000036512 infertility Effects 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 238000001155 isoelectric focusing Methods 0.000 description 1
- 208000032839 leukemia Diseases 0.000 description 1
- 239000003446 ligand Substances 0.000 description 1
- 125000003473 lipid group Chemical group 0.000 description 1
- 239000012092 media component Substances 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- XYJRXVWERLGGKC-UHFFFAOYSA-D pentacalcium;hydroxide;triphosphate Chemical compound [OH-].[Ca+2].[Ca+2].[Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O XYJRXVWERLGGKC-UHFFFAOYSA-D 0.000 description 1
- 230000003449 preventive effect Effects 0.000 description 1
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 1
- XNSAINXGIQZQOO-SRVKXCTJSA-N protirelin Chemical compound NC(=O)[C@@H]1CCCN1C(=O)[C@@H](NC(=O)[C@H]1NC(=O)CC1)CC1=CN=CN1 XNSAINXGIQZQOO-SRVKXCTJSA-N 0.000 description 1
- 239000002510 pyrogen Substances 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- 239000012679 serum free medium Substances 0.000 description 1
- 239000000741 silica gel Substances 0.000 description 1
- 229910002027 silica gel Inorganic materials 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 238000002054 transplantation Methods 0.000 description 1
- 230000003612 virological effect Effects 0.000 description 1
- 235000013343 vitamin Nutrition 0.000 description 1
- 239000011782 vitamin Substances 0.000 description 1
- 229940088594 vitamin Drugs 0.000 description 1
- 229930003231 vitamin Natural products 0.000 description 1
- 238000001262 western blot Methods 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
- C07K16/065—Purification, fragmentation
Landscapes
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Health & Medical Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Life Sciences & Earth Sciences (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Immunology (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| DE4118912A DE4118912C1 (enExample) | 1991-06-08 | 1991-06-08 | |
| DE4118912:4 | 1991-06-08 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPH07267997A JPH07267997A (ja) | 1995-10-17 |
| JP2644946B2 true JP2644946B2 (ja) | 1997-08-25 |
Family
ID=6433511
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP4145807A Expired - Fee Related JP2644946B2 (ja) | 1991-06-08 | 1992-06-05 | ＩｇＧ− モノクロナール抗体の精製方法及びその使用方法 |
Country Status (7)
| Country | Link |
|---|---|
| EP (1) | EP0530447B1 (enExample) |
| JP (1) | JP2644946B2 (enExample) |
| AT (1) | ATE159532T1 (enExample) |
| DE (2) | DE4118912C1 (enExample) |
| DK (1) | DK0530447T3 (enExample) |
| ES (1) | ES2108059T3 (enExample) |
| GR (1) | GR3025603T3 (enExample) |
Families Citing this family (24)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| FR2706466B1 (fr) * | 1993-06-14 | 1995-08-25 | Aetsrn | Concentré d'immunoglobulines G à usage thérapeutique et procédé de production dudit concentré. |
| IL121900A (en) * | 1997-10-07 | 2001-12-23 | Omrix Biopharmaceuticals Ltd | A method for the purification of immunoglobulins |
| DK2270044T3 (en) | 1998-06-09 | 2015-01-26 | Csl Behring Ag | Liquid immunoglobulin G (IgG) product |
| SK288128B6 (sk) * | 1998-06-09 | 2013-10-02 | Csl Behring Ag | Process for purifying immunoglobulin G (IgG), liquid immunoglobulin product and use thereof for the preparation of a medicament |
| SE0001128D0 (sv) * | 2000-03-30 | 2000-03-30 | Amersham Pharm Biotech Ab | A method of producing IgG |
| WO2004087761A1 (ja) * | 2003-03-31 | 2004-10-14 | Kirin Beer Kabushiki Kaisha | ヒトモノクローナル抗体およびヒトポリクローナル抗体の精製 |
| EP1532983A1 (en) | 2003-11-18 | 2005-05-25 | ZLB Bioplasma AG | Immunoglobulin preparations having increased stability |
| TWI391399B (zh) | 2005-05-25 | 2013-04-01 | Hoffmann La Roche | 測定溶離多肽之鹽濃度之方法 |
| AU2008256411B2 (en) | 2007-06-01 | 2013-08-22 | F. Hoffmann-La Roche Ag | Immunoglobulin purification |
| CL2008002054A1 (es) | 2007-07-17 | 2009-05-29 | Hoffmann La Roche | Metodo para la regeneracion de una columna de cromatografia de intercambio cationico despues de la elusion de eritropoyetina monopeguilada y metodo para obtener una eritropoyetina monopeguilada, incorporando el metodo de regeneracion de la columna de intercambio cationico. |
| AR067537A1 (es) | 2007-07-17 | 2009-10-14 | Hoffmann La Roche | Purificacion de polipeptidos pegilados |
| WO2009058769A1 (en) * | 2007-10-30 | 2009-05-07 | Schering Corporation | Purification of antibodies containing hydrophobic variants |
| CN102264392A (zh) | 2008-12-22 | 2011-11-30 | 弗·哈夫曼-拉罗切有限公司 | 免疫球蛋白纯化 |
| PL2531218T3 (pl) | 2010-02-04 | 2019-05-31 | Csl Behring Ag | Preparat immunoglobuliny |
| JP2013519652A (ja) * | 2010-02-12 | 2013-05-30 | ディーエスエム アイピー アセッツ ビー．ブイ． | 単一ユニット抗体精製 |
| EP2361636A1 (en) | 2010-02-26 | 2011-08-31 | CSL Behring AG | Immunoglobulin preparation and storage system for an immunoglobulin preparation |
| EP2616101B1 (en) | 2010-09-14 | 2014-07-09 | F.Hoffmann-La Roche Ag | Method for purifying pegylated erythropoietin |
| WO2012059308A1 (en) * | 2010-11-01 | 2012-05-10 | Dsm Ip Assets B.V. | Single unit ion exchange chromatography antibody purification |
| EP2748178B1 (en) | 2011-08-25 | 2018-10-31 | F. Hoffmann-La Roche AG | Cation and anion exchange chromatography method |
| ES2546064T3 (es) * | 2011-11-22 | 2015-09-18 | Heraeus Medical Gmbh | Esterilización de monómeros polimerizables |
| CN106459140B (zh) * | 2014-03-11 | 2019-12-10 | 株式会社绿十字控股 | 用于纯化免疫球蛋白的方法 |
| HUE052280T2 (hu) | 2014-12-03 | 2021-04-28 | Csl Behring Ag | Immunoglobulinokat tartalmazó megnövelt stabilitású gyógyszerészeti termék |
| MX391087B (es) | 2016-07-15 | 2025-03-21 | Hoffmann La Roche | Método para purificar eritropoyetina pegilada. |
| AU2020216368B2 (en) * | 2019-01-30 | 2025-04-24 | Amgen Inc. | Aflibercept attributes and methods of characterizing and modifying thereof |
Family Cites Families (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4469630A (en) * | 1983-11-25 | 1984-09-04 | J. T. Baker Chemical Co. | Purification of monoclonal antibodies |
| US4743680A (en) * | 1985-02-01 | 1988-05-10 | New York University | Method for purifying antihemophilic factor |
| DE3640513A1 (de) * | 1986-11-27 | 1988-06-09 | Biotest Pharma Gmbh | Verfahren zur herstellung eines virussicheren, lagerstabilen und intravenoes vertraeglichen immunglobulin-g-praeparates |
| DE3641115A1 (de) * | 1986-12-02 | 1988-06-16 | Lentia Gmbh | Verfahren zur herstellung eines intravenoes anwendbaren und in fluessiger form stabilen immunglobulins |
| CA1323567C (en) * | 1987-10-05 | 1993-10-26 | Gene R. Nathans | Method for purification of antibodies |
| US5118796A (en) * | 1987-12-09 | 1992-06-02 | Centocor, Incorporated | Efficient large-scale purification of immunoglobulins and derivatives |
| CA2005600A1 (en) * | 1988-12-20 | 1990-06-20 | Cal-Henrik Heldin | Endothelial cell growth factor |
-
1991
- 1991-06-08 DE DE4118912A patent/DE4118912C1/de not_active Expired - Fee Related
-
1992
- 1992-05-27 EP EP92108912A patent/EP0530447B1/de not_active Expired - Lifetime
- 1992-05-27 ES ES92108912T patent/ES2108059T3/es not_active Expired - Lifetime
- 1992-05-27 DE DE59208982T patent/DE59208982D1/de not_active Expired - Lifetime
- 1992-05-27 DK DK92108912.4T patent/DK0530447T3/da active
- 1992-05-27 AT AT92108912T patent/ATE159532T1/de active
- 1992-06-05 JP JP4145807A patent/JP2644946B2/ja not_active Expired - Fee Related
-
1997
- 1997-12-05 GR GR970403248T patent/GR3025603T3/el unknown
Also Published As
| Publication number | Publication date |
|---|---|
| JPH07267997A (ja) | 1995-10-17 |
| GR3025603T3 (en) | 1998-03-31 |
| EP0530447B1 (de) | 1997-10-22 |
| ES2108059T3 (es) | 1997-12-16 |
| EP0530447A2 (de) | 1993-03-10 |
| DK0530447T3 (da) | 1998-01-12 |
| DE4118912C1 (enExample) | 1992-07-02 |
| EP0530447A3 (en) | 1993-08-18 |
| DE59208982D1 (de) | 1997-11-27 |
| ATE159532T1 (de) | 1997-11-15 |
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