JP2002541155A - 生物学的調製物の精製 - Google Patents
生物学的調製物の精製Info
- Publication number
- JP2002541155A JP2002541155A JP2000609437A JP2000609437A JP2002541155A JP 2002541155 A JP2002541155 A JP 2002541155A JP 2000609437 A JP2000609437 A JP 2000609437A JP 2000609437 A JP2000609437 A JP 2000609437A JP 2002541155 A JP2002541155 A JP 2002541155A
- Authority
- JP
- Japan
- Prior art keywords
- endotoxin
- hydrophobic
- biological material
- protein
- charged
- 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.)
- Pending
Links
- 238000000746 purification Methods 0.000 title abstract description 16
- 238000002360 preparation method Methods 0.000 title abstract description 10
- 238000000034 method Methods 0.000 claims abstract description 30
- 239000000356 contaminant Substances 0.000 claims abstract description 11
- 239000002158 endotoxin Substances 0.000 claims description 62
- 239000012620 biological material Substances 0.000 claims description 34
- 230000002209 hydrophobic effect Effects 0.000 claims description 25
- 150000003839 salts Chemical class 0.000 claims description 21
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 claims description 18
- 229910052921 ammonium sulfate Inorganic materials 0.000 claims description 18
- 235000011130 ammonium sulphate Nutrition 0.000 claims description 18
- 239000003795 chemical substances by application Substances 0.000 claims description 13
- 239000007790 solid phase Substances 0.000 claims description 13
- 230000002934 lysing effect Effects 0.000 claims description 12
- 239000000463 material Substances 0.000 claims description 12
- 239000011159 matrix material Substances 0.000 claims description 8
- 229960000789 guanidine hydrochloride Drugs 0.000 claims description 6
- PJJJBBJSCAKJQF-UHFFFAOYSA-N guanidinium chloride Chemical compound [Cl-].NC(N)=[NH2+] PJJJBBJSCAKJQF-UHFFFAOYSA-N 0.000 claims description 6
- 239000000126 substance Substances 0.000 claims description 6
- 125000001997 phenyl group Chemical group [H]C1=C([H])C([H])=C(*)C([H])=C1[H] 0.000 claims description 5
- 239000004094 surface-active agent Substances 0.000 claims description 5
- 238000004440 column chromatography Methods 0.000 claims description 3
- 125000001165 hydrophobic group Chemical group 0.000 claims description 3
- ZMZDMBWJUHKJPS-UHFFFAOYSA-M Thiocyanate anion Chemical compound [S-]C#N ZMZDMBWJUHKJPS-UHFFFAOYSA-M 0.000 claims description 2
- 239000011543 agarose gel Substances 0.000 claims description 2
- ZMZDMBWJUHKJPS-UHFFFAOYSA-N hydrogen thiocyanate Natural products SC#N ZMZDMBWJUHKJPS-UHFFFAOYSA-N 0.000 claims description 2
- 238000005185 salting out Methods 0.000 claims description 2
- 230000001376 precipitating effect Effects 0.000 claims 1
- 108090000623 proteins and genes Proteins 0.000 abstract description 47
- 102000004169 proteins and genes Human genes 0.000 abstract description 47
- 241000894006 Bacteria Species 0.000 abstract description 8
- 108020004707 nucleic acids Proteins 0.000 abstract description 6
- 102000039446 nucleic acids Human genes 0.000 abstract description 6
- 150000007523 nucleic acids Chemical class 0.000 abstract description 6
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 abstract description 5
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 abstract description 5
- 108020004511 Recombinant DNA Proteins 0.000 abstract description 2
- 235000018102 proteins Nutrition 0.000 description 45
- 235000002639 sodium chloride Nutrition 0.000 description 26
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 16
- 241000588724 Escherichia coli Species 0.000 description 14
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 13
- 235000018417 cysteine Nutrition 0.000 description 13
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 12
- 108020001507 fusion proteins Proteins 0.000 description 12
- 102000037865 fusion proteins Human genes 0.000 description 12
- 239000000872 buffer Substances 0.000 description 11
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 10
- 239000004202 carbamide Substances 0.000 description 10
- 239000008188 pellet Substances 0.000 description 10
- 238000000926 separation method Methods 0.000 description 9
- 238000011109 contamination Methods 0.000 description 8
- 239000011780 sodium chloride Substances 0.000 description 8
- 238000012360 testing method Methods 0.000 description 7
- 108020004414 DNA Proteins 0.000 description 6
- 239000004471 Glycine Substances 0.000 description 6
- 229920002684 Sepharose Polymers 0.000 description 6
- 210000004027 cell Anatomy 0.000 description 6
- 239000000047 product Substances 0.000 description 6
- 229960005486 vaccine Drugs 0.000 description 6
- 238000005119 centrifugation Methods 0.000 description 5
- 108090000765 processed proteins & peptides Proteins 0.000 description 5
- 229920005654 Sephadex Polymers 0.000 description 4
- 239000002671 adjuvant Substances 0.000 description 4
- 238000005571 anion exchange chromatography Methods 0.000 description 4
- 239000000427 antigen Substances 0.000 description 4
- 108091007433 antigens Proteins 0.000 description 4
- 102000036639 antigens Human genes 0.000 description 4
- 238000001914 filtration Methods 0.000 description 4
- 210000003000 inclusion body Anatomy 0.000 description 4
- 239000008363 phosphate buffer Substances 0.000 description 4
- 239000000243 solution Substances 0.000 description 4
- 239000013589 supplement Substances 0.000 description 4
- 229910019142 PO4 Inorganic materials 0.000 description 3
- 239000012507 Sephadex™ Substances 0.000 description 3
- 125000000217 alkyl group Chemical group 0.000 description 3
- 238000004587 chromatography analysis Methods 0.000 description 3
- 239000012141 concentrate Substances 0.000 description 3
- 239000003814 drug Substances 0.000 description 3
- 238000010828 elution Methods 0.000 description 3
- 238000011013 endotoxin removal Methods 0.000 description 3
- 238000009472 formulation Methods 0.000 description 3
- 238000002523 gelfiltration Methods 0.000 description 3
- 230000003993 interaction Effects 0.000 description 3
- 229920006008 lipopolysaccharide Polymers 0.000 description 3
- 238000005374 membrane filtration Methods 0.000 description 3
- 239000000203 mixture Substances 0.000 description 3
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 3
- 239000010452 phosphate Substances 0.000 description 3
- 230000000717 retained effect Effects 0.000 description 3
- 238000001179 sorption measurement Methods 0.000 description 3
- 239000006228 supernatant Substances 0.000 description 3
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 2
- NTYJJOPFIAHURM-UHFFFAOYSA-N Histamine Chemical compound NCCC1=CN=CN1 NTYJJOPFIAHURM-UHFFFAOYSA-N 0.000 description 2
- 241000701806 Human papillomavirus Species 0.000 description 2
- 108010040201 Polymyxins Proteins 0.000 description 2
- 102000007562 Serum Albumin Human genes 0.000 description 2
- 108010071390 Serum Albumin Proteins 0.000 description 2
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 2
- 239000007983 Tris buffer Substances 0.000 description 2
- -1 agarose or dextran Chemical class 0.000 description 2
- 238000005349 anion exchange Methods 0.000 description 2
- 239000011324 bead Substances 0.000 description 2
- 125000004432 carbon atom Chemical group C* 0.000 description 2
- 238000005277 cation exchange chromatography Methods 0.000 description 2
- WOWHHFRSBJGXCM-UHFFFAOYSA-M cetyltrimethylammonium chloride Chemical compound [Cl-].CCCCCCCCCCCCCCCC[N+](C)(C)C WOWHHFRSBJGXCM-UHFFFAOYSA-M 0.000 description 2
- 238000011026 diafiltration Methods 0.000 description 2
- 239000012149 elution buffer Substances 0.000 description 2
- 239000000499 gel Substances 0.000 description 2
- 239000012528 membrane Substances 0.000 description 2
- 239000002245 particle Substances 0.000 description 2
- 229920000642 polymer Polymers 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 239000002594 sorbent Substances 0.000 description 2
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 2
- 230000003612 virological effect Effects 0.000 description 2
- BFSVOASYOCHEOV-UHFFFAOYSA-N 2-diethylaminoethanol Chemical compound CCN(CC)CCO BFSVOASYOCHEOV-UHFFFAOYSA-N 0.000 description 1
- HRPVXLWXLXDGHG-UHFFFAOYSA-N Acrylamide Chemical compound NC(=O)C=C HRPVXLWXLXDGHG-UHFFFAOYSA-N 0.000 description 1
- 229920000936 Agarose Polymers 0.000 description 1
- 108010088751 Albumins Proteins 0.000 description 1
- 102000009027 Albumins Human genes 0.000 description 1
- 231100000699 Bacterial toxin Toxicity 0.000 description 1
- 102000016938 Catalase Human genes 0.000 description 1
- 108010053835 Catalase Proteins 0.000 description 1
- 229920002307 Dextran Polymers 0.000 description 1
- 241000341655 Human papillomavirus type 16 Species 0.000 description 1
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 1
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 241000863393 Methylophilus methylotrophus Species 0.000 description 1
- 102000016943 Muramidase Human genes 0.000 description 1
- 108010014251 Muramidase Proteins 0.000 description 1
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
- 238000000636 Northern blotting Methods 0.000 description 1
- 108091005461 Nucleic proteins Proteins 0.000 description 1
- 241001631646 Papillomaviridae Species 0.000 description 1
- YNPNZTXNASCQKK-UHFFFAOYSA-N Phenanthrene Natural products C1=CC=C2C3=CC=CC=C3C=CC2=C1 YNPNZTXNASCQKK-UHFFFAOYSA-N 0.000 description 1
- 239000004952 Polyamide Substances 0.000 description 1
- 108010093965 Polymyxin B Proteins 0.000 description 1
- 241000589516 Pseudomonas Species 0.000 description 1
- 206010037660 Pyrexia Diseases 0.000 description 1
- 241000219492 Quercus Species 0.000 description 1
- PMZURENOXWZQFD-UHFFFAOYSA-L Sodium Sulfate Chemical compound [Na+].[Na+].[O-]S([O-])(=O)=O PMZURENOXWZQFD-UHFFFAOYSA-L 0.000 description 1
- 238000002105 Southern blotting Methods 0.000 description 1
- 239000013504 Triton X-100 Substances 0.000 description 1
- 229920004890 Triton X-100 Polymers 0.000 description 1
- 241000607598 Vibrio Species 0.000 description 1
- DGEZNRSVGBDHLK-UHFFFAOYSA-N [1,10]phenanthroline Chemical compound C1=CN=C2C3=NC=CC=C3C=CC2=C1 DGEZNRSVGBDHLK-UHFFFAOYSA-N 0.000 description 1
- 238000001261 affinity purification Methods 0.000 description 1
- 229940037003 alum Drugs 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 239000008346 aqueous phase Substances 0.000 description 1
- 125000003118 aryl group Chemical group 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 239000000688 bacterial toxin Substances 0.000 description 1
- 238000004166 bioassay Methods 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 239000006285 cell suspension Substances 0.000 description 1
- 210000002421 cell wall Anatomy 0.000 description 1
- RLGQACBPNDBWTB-UHFFFAOYSA-N cetyltrimethylammonium ion Chemical compound CCCCCCCCCCCCCCCC[N+](C)(C)C RLGQACBPNDBWTB-UHFFFAOYSA-N 0.000 description 1
- 229920001577 copolymer Polymers 0.000 description 1
- 239000003398 denaturant Substances 0.000 description 1
- 238000001212 derivatisation Methods 0.000 description 1
- MOTZDAYCYVMXPC-UHFFFAOYSA-N dodecyl hydrogen sulfate Chemical compound CCCCCCCCCCCCOS(O)(=O)=O MOTZDAYCYVMXPC-UHFFFAOYSA-N 0.000 description 1
- 229940043264 dodecyl sulfate Drugs 0.000 description 1
- 238000011143 downstream manufacturing Methods 0.000 description 1
- 239000006167 equilibration buffer Substances 0.000 description 1
- 239000000706 filtrate Substances 0.000 description 1
- 125000000524 functional group Chemical group 0.000 description 1
- 108010074605 gamma-Globulins Proteins 0.000 description 1
- 238000001415 gene therapy Methods 0.000 description 1
- 150000004676 glycans Chemical class 0.000 description 1
- 239000008062 guanidine hydrochloride buffer Substances 0.000 description 1
- ISNICOKBNZOJQG-UHFFFAOYSA-O guanidinium ion Chemical compound C[NH+]=C(N(C)C)N(C)C ISNICOKBNZOJQG-UHFFFAOYSA-O 0.000 description 1
- 229960001340 histamine Drugs 0.000 description 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
- 229960002885 histidine Drugs 0.000 description 1
- 238000004191 hydrophobic interaction chromatography Methods 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 230000002452 interceptive effect Effects 0.000 description 1
- 230000002535 lyotropic effect Effects 0.000 description 1
- 229960000274 lysozyme Drugs 0.000 description 1
- 235000010335 lysozyme Nutrition 0.000 description 1
- 239000004325 lysozyme Substances 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 229920002647 polyamide Polymers 0.000 description 1
- 229920000024 polymyxin B Polymers 0.000 description 1
- 229960005266 polymyxin b Drugs 0.000 description 1
- 229920001282 polysaccharide Polymers 0.000 description 1
- 239000005017 polysaccharide Substances 0.000 description 1
- 229920003053 polystyrene-divinylbenzene Polymers 0.000 description 1
- 102000004196 processed proteins & peptides Human genes 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 230000000069 prophylactic effect Effects 0.000 description 1
- 239000012460 protein solution Substances 0.000 description 1
- 239000012264 purified product Substances 0.000 description 1
- 230000001698 pyrogenic effect Effects 0.000 description 1
- 125000001453 quaternary ammonium group Chemical group 0.000 description 1
- 229910052938 sodium sulfate Inorganic materials 0.000 description 1
- 235000011152 sodium sulphate Nutrition 0.000 description 1
- VGTPCRGMBIAPIM-UHFFFAOYSA-M sodium thiocyanate Chemical compound [Na+].[S-]C#N VGTPCRGMBIAPIM-UHFFFAOYSA-M 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 239000007858 starting material Substances 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 238000010998 test method Methods 0.000 description 1
- 230000001225 therapeutic effect Effects 0.000 description 1
- 239000003053 toxin Substances 0.000 description 1
- 231100000765 toxin Toxicity 0.000 description 1
- 108700012359 toxins Proteins 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 238000001262 western blot 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
- C07K1/16—Extraction; Separation; Purification by chromatography
- C07K1/20—Partition-, reverse-phase or hydrophobic interaction chromatography
Landscapes
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Analytical Chemistry (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GB9907553.3 | 1999-04-01 | ||
| GBGB9907553.3A GB9907553D0 (en) | 1999-04-01 | 1999-04-01 | Purification of biological preparations |
| PCT/GB2000/001256 WO2000059927A1 (en) | 1999-04-01 | 2000-04-03 | Purification of biological preparations |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JP2002541155A true JP2002541155A (ja) | 2002-12-03 |
| JP2002541155A5 JP2002541155A5 (https=) | 2007-05-31 |
Family
ID=10850819
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2000609437A Pending JP2002541155A (ja) | 1999-04-01 | 2000-04-03 | 生物学的調製物の精製 |
Country Status (7)
| Country | Link |
|---|---|
| US (1) | US6310186B1 (https=) |
| EP (1) | EP1165599A1 (https=) |
| JP (1) | JP2002541155A (https=) |
| AU (1) | AU3569600A (https=) |
| CA (1) | CA2365513A1 (https=) |
| GB (1) | GB9907553D0 (https=) |
| WO (1) | WO2000059927A1 (https=) |
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2012530488A (ja) * | 2009-06-19 | 2012-12-06 | アイジェン インコーポレーテッド | 子宮頸がんワクチン |
| JP2017206529A (ja) * | 2009-08-06 | 2017-11-24 | ジェネンテック， インコーポレイテッド | タンパク質精製におけるウイルス除去の改良方法 |
Families Citing this family (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| AU6124201A (en) * | 2000-05-03 | 2001-11-12 | Expressive Constructs Inc | A method and device for improving protein stability and solubility |
| EP1578763B1 (en) * | 2002-12-23 | 2009-01-07 | Vical Incorporated | Process for purification of plasmid dna |
| EP1624886A2 (en) * | 2003-05-12 | 2006-02-15 | Expressive Constructs, Inc. | Methods for increasing cell and tissue viability |
| US6913695B2 (en) * | 2003-07-08 | 2005-07-05 | Bayer Healthcare Llc | Sanitization of chromatographic media |
| DE602004026343D1 (de) | 2003-10-24 | 2010-05-12 | Amgen Inc | Verfahren zur aufreinigung von proteinen in einer durchflussfraktion aus der chromatographie mit hydrophoben wechselwirkungen |
| JP2010520320A (ja) | 2007-02-28 | 2010-06-10 | リポクセン テクノロジーズ リミテッド | ポリシアル酸におけるエンドトキシンの低減 |
| WO2015128788A1 (en) * | 2014-02-27 | 2015-09-03 | Shantha Biotechnics Private Limited | Purification of papillomavirus l2 protein |
Family Cites Families (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS5951220A (ja) * | 1982-08-02 | 1984-03-24 | Asahi Chem Ind Co Ltd | 新規なプラスミノ−ゲン・アクチベ−タ−およびその製法ならびにこれを含有する薬剤 |
| US4707542A (en) * | 1983-08-22 | 1987-11-17 | Merck & Co., Inc. | Immunogenic HbsAg derived from transformed yeast |
| US4894439A (en) * | 1986-05-22 | 1990-01-16 | Cetus Corporation | N-terminal derivatives of tumor necrosis factor purified by microporous PTFE membranes |
| US5200509A (en) * | 1987-04-06 | 1993-04-06 | Celtrix Pharmaceuticals, Inc. | Human somatomedin carrier protein subunits and process for producing them; recombinant DNA molecules, hosts, processes and human somatomedin carrier protein-like polypeptides |
| EP0330700B1 (en) * | 1987-08-19 | 1993-12-22 | Sagami Chemical Research Center | Human prourokinase-like polypeptide |
| JPH01238534A (ja) * | 1988-03-17 | 1989-09-22 | Mitsui Toatsu Chem Inc | エンドトキシンの除去方法 |
| US5429746A (en) * | 1994-02-22 | 1995-07-04 | Smith Kline Beecham Corporation | Antibody purification |
-
1999
- 1999-04-01 GB GBGB9907553.3A patent/GB9907553D0/en not_active Ceased
-
2000
- 2000-04-03 EP EP00914302A patent/EP1165599A1/en not_active Withdrawn
- 2000-04-03 JP JP2000609437A patent/JP2002541155A/ja active Pending
- 2000-04-03 AU AU35696/00A patent/AU3569600A/en not_active Abandoned
- 2000-04-03 CA CA002365513A patent/CA2365513A1/en not_active Abandoned
- 2000-04-03 WO PCT/GB2000/001256 patent/WO2000059927A1/en not_active Ceased
- 2000-04-03 US US09/541,815 patent/US6310186B1/en not_active Expired - Fee Related
Cited By (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2012530488A (ja) * | 2009-06-19 | 2012-12-06 | アイジェン インコーポレーテッド | 子宮頸がんワクチン |
| JP2017206529A (ja) * | 2009-08-06 | 2017-11-24 | ジェネンテック， インコーポレイテッド | タンパク質精製におけるウイルス除去の改良方法 |
| US11225513B2 (en) | 2009-08-06 | 2022-01-18 | Genentech, Inc. | Method to improve virus filtration capacity |
| JP2025003999A (ja) * | 2009-08-06 | 2025-01-14 | ジェネンテック， インコーポレイテッド | タンパク質精製におけるウイルス除去の改良方法 |
Also Published As
| Publication number | Publication date |
|---|---|
| EP1165599A1 (en) | 2002-01-02 |
| AU3569600A (en) | 2000-10-23 |
| GB9907553D0 (en) | 1999-05-26 |
| CA2365513A1 (en) | 2000-10-12 |
| US6310186B1 (en) | 2001-10-30 |
| WO2000059927A1 (en) | 2000-10-12 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| JP4198751B2 (ja) | 抗体の精製 | |
| EP3663401B1 (en) | Purification process for biological molecules such as plasmid dna using anionic exchange chromatography | |
| EP2961761B1 (en) | Protein purification in the presence of nonionic organic polymers at elevated conductivity | |
| EP2854980B1 (en) | Selective binding of biological targets to solid phase ureides | |
| Wilson et al. | Removal of tightly bound endotoxin from biological products | |
| US9902942B2 (en) | Chromatographic purification of virus preparations with negatively charged particles | |
| JP6385374B2 (ja) | タンパク質製剤からエンドトキシンを除去するための物質および方法 | |
| CN105008383A (zh) | 在非离子有机聚合物和正电性表面存在下的蛋白质纯化 | |
| US12492383B2 (en) | Method for depletion or removal of endotoxin from an endotoxin-containing source or potentially endotoxin-containing source | |
| CN116234619A (zh) | 宿主细胞dna的金属亲和提取 | |
| JP2002541155A (ja) | 生物学的調製物の精製 | |
| EP2012118A1 (en) | SEPARATING AGENT FOR IgG PURIFICATION, AND METHOD FOR PURIFYING AN IgG MONOMER USING IT | |
| US4485038A (en) | Method for the production and purification of human leukocyte interferon | |
| EP0252588A2 (en) | Process for the isolation and purification of P. falciparum CS protein expressed in recombinant E. coli, and its use as a vaccine | |
| JP2002541155A5 (https=) | ||
| US20230227791A1 (en) | Enhanced purification of adeno-associated virus to more effectively remove contaminating dna | |
| JP2003514655A (ja) | 核酸構造を有する化合物を含むサンプル由来の物質の選択的除去方法 | |
| EP4025584A1 (en) | Compositions and methods for reducing chromatin content of biological preparations | |
| JP5137491B2 (ja) | 水酸化アルミニウム吸着体の吸着性及び／又は溶出性の改変方法 | |
| US11732004B2 (en) | Compositions and methods for simplified high efficiency isolation of proteins | |
| JPS62259596A (ja) | ハイブリツドタンパク質の精製方法 | |
| WO1991018009A1 (en) | A process for the purification of proteins |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20070403 |
|
| A621 | Written request for application examination |
Free format text: JAPANESE INTERMEDIATE CODE: A621 Effective date: 20070403 |
|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20091117 |
|
| A02 | Decision of refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A02 Effective date: 20100427 |