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 (enExample) | 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 (enExample) |
| EP (1) | EP1165599A1 (enExample) |
| JP (1) | JP2002541155A (enExample) |
| AU (1) | AU3569600A (enExample) |
| CA (1) | CA2365513A1 (enExample) |
| GB (1) | GB9907553D0 (enExample) |
| WO (1) | WO2000059927A1 (enExample) |
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 |
| CA2542951C (en) * | 2003-10-24 | 2016-08-30 | Abhinav A. Shukla | Process for purifying proteins in a hydrophobic interaction chromatography flow-through fraction |
| DK2115010T3 (da) * | 2007-02-28 | 2012-02-06 | Lipoxen Technologies Ltd | Mindskelse af endotoksin i polysialinsyrer |
| 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 |
| DE3886517T2 (de) * | 1987-08-19 | 1994-04-21 | Central Glass Co Ltd | Menschlicher Prourokinase ähnliches Polypeptid. |
| 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 US US09/541,815 patent/US6310186B1/en not_active Expired - Fee Related
- 2000-04-03 CA CA002365513A patent/CA2365513A1/en not_active Abandoned
- 2000-04-03 AU AU35696/00A patent/AU3569600A/en not_active Abandoned
- 2000-04-03 JP JP2000609437A patent/JP2002541155A/ja active Pending
- 2000-04-03 WO PCT/GB2000/001256 patent/WO2000059927A1/en not_active Ceased
- 2000-04-03 EP EP00914302A patent/EP1165599A1/en not_active Withdrawn
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 |
|---|---|
| AU3569600A (en) | 2000-10-23 |
| EP1165599A1 (en) | 2002-01-02 |
| US6310186B1 (en) | 2001-10-30 |
| WO2000059927A1 (en) | 2000-10-12 |
| CA2365513A1 (en) | 2000-10-12 |
| GB9907553D0 (en) | 1999-05-26 |
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Legal Events
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| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20070403 |
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| A621 | Written request for application examination |
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| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20091117 |
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| A02 | Decision of refusal |
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