JP2004520056A5 - - Google Patents
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- Publication number
- JP2004520056A5 JP2004520056A5 JP2002566373A JP2002566373A JP2004520056A5 JP 2004520056 A5 JP2004520056 A5 JP 2004520056A5 JP 2002566373 A JP2002566373 A JP 2002566373A JP 2002566373 A JP2002566373 A JP 2002566373A JP 2004520056 A5 JP2004520056 A5 JP 2004520056A5
- Authority
- JP
- Japan
- Prior art keywords
- nucleic acid
- fusion
- fusion protein
- protease
- ssao
- 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
- 102000037865 fusion proteins Human genes 0.000 claims description 27
- 108020001507 fusion proteins Proteins 0.000 claims description 27
- 230000004927 fusion Effects 0.000 claims description 23
- 230000000694 effects Effects 0.000 claims description 21
- 108091005804 Peptidases Proteins 0.000 claims description 16
- 239000004365 Protease Substances 0.000 claims description 16
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims description 16
- 238000000034 method Methods 0.000 claims description 12
- 239000013604 expression vector Substances 0.000 claims description 11
- 238000003776 cleavage reaction Methods 0.000 claims description 10
- 239000001963 growth medium Substances 0.000 claims description 10
- 230000007017 scission Effects 0.000 claims description 10
- 238000000746 purification Methods 0.000 claims description 8
- 108010079340 Benzylamine Oxidase Proteins 0.000 claims description 5
- 238000004519 manufacturing process Methods 0.000 claims description 2
- 108020004707 nucleic acids Proteins 0.000 claims 17
- 102000039446 nucleic acids Human genes 0.000 claims 17
- 150000007523 nucleic acids Chemical class 0.000 claims 17
- 101000694615 Homo sapiens Membrane primary amine oxidase Proteins 0.000 claims 13
- 150000001413 amino acids Chemical class 0.000 claims 6
- 239000003446 ligand Substances 0.000 claims 5
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 claims 3
- 108010076504 Protein Sorting Signals Proteins 0.000 claims 3
- 235000001014 amino acid Nutrition 0.000 claims 3
- 102000005720 Glutathione transferase Human genes 0.000 claims 2
- 108010070675 Glutathione transferase Proteins 0.000 claims 2
- 238000012258 culturing Methods 0.000 claims 2
- RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical group OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 claims 2
- 108010091324 3C proteases Proteins 0.000 claims 1
- 108010024636 Glutathione Proteins 0.000 claims 1
- 241000709664 Picornaviridae Species 0.000 claims 1
- 241000242677 Schistosoma japonicum Species 0.000 claims 1
- 125000000539 amino acid group Chemical group 0.000 claims 1
- 230000008878 coupling Effects 0.000 claims 1
- 238000010168 coupling process Methods 0.000 claims 1
- 238000005859 coupling reaction Methods 0.000 claims 1
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 claims 1
- 238000006471 dimerization reaction Methods 0.000 claims 1
- 239000012634 fragment Substances 0.000 claims 1
- 229960003180 glutathione Drugs 0.000 claims 1
- 230000003100 immobilizing effect Effects 0.000 claims 1
- 239000002773 nucleotide Substances 0.000 claims 1
- 125000003729 nucleotide group Chemical group 0.000 claims 1
- 230000028327 secretion Effects 0.000 claims 1
- 210000004027 cell Anatomy 0.000 description 10
- 235000018102 proteins Nutrition 0.000 description 10
- 102000004169 proteins and genes Human genes 0.000 description 10
- 108090000623 proteins and genes Proteins 0.000 description 10
- 239000003636 conditioned culture medium Substances 0.000 description 7
- 102000004190 Enzymes Human genes 0.000 description 5
- 108090000790 Enzymes Proteins 0.000 description 5
- 229920002684 Sepharose Polymers 0.000 description 5
- 238000004458 analytical method Methods 0.000 description 5
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 4
- 239000011324 bead Substances 0.000 description 4
- BRZYSWJRSDMWLG-CAXSIQPQSA-N geneticin Chemical compound O1C[C@@](O)(C)[C@H](NC)[C@@H](O)[C@H]1O[C@@H]1[C@@H](O)[C@H](O[C@@H]2[C@@H]([C@@H](O)[C@H](O)[C@@H](C(C)O)O2)N)[C@@H](N)C[C@H]1N BRZYSWJRSDMWLG-CAXSIQPQSA-N 0.000 description 4
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 4
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 3
- 239000012091 fetal bovine serum Substances 0.000 description 3
- 108010028700 Amine Oxidase (Copper-Containing) Proteins 0.000 description 2
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 2
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 2
- WGQKYBSKWIADBV-UHFFFAOYSA-N benzylamine Chemical compound NCC1=CC=CC=C1 WGQKYBSKWIADBV-UHFFFAOYSA-N 0.000 description 2
- 238000012512 characterization method Methods 0.000 description 2
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 2
- 235000018417 cysteine Nutrition 0.000 description 2
- 238000001514 detection method Methods 0.000 description 2
- 206010012601 diabetes mellitus Diseases 0.000 description 2
- 230000035772 mutation Effects 0.000 description 2
- 239000011780 sodium chloride Substances 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- 238000001890 transfection Methods 0.000 description 2
- 230000002792 vascular Effects 0.000 description 2
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 1
- 102000016893 Amine Oxidase (Copper-Containing) Human genes 0.000 description 1
- 201000001320 Atherosclerosis Diseases 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 208000024172 Cardiovascular disease Diseases 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
- 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 1
- 241000206602 Eukaryota Species 0.000 description 1
- 102000008857 Ferritin Human genes 0.000 description 1
- 108050000784 Ferritin Proteins 0.000 description 1
- 238000008416 Ferritin Methods 0.000 description 1
- 102000001390 Fructose-Bisphosphate Aldolase Human genes 0.000 description 1
- 108010068561 Fructose-Bisphosphate Aldolase Proteins 0.000 description 1
- 206010019280 Heart failures Diseases 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 1
- 229930182816 L-glutamine Natural products 0.000 description 1
- 102100027159 Membrane primary amine oxidase Human genes 0.000 description 1
- 108090000854 Oxidoreductases Proteins 0.000 description 1
- 102000004316 Oxidoreductases Human genes 0.000 description 1
- 102000003992 Peroxidases Human genes 0.000 description 1
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
- 239000012505 Superdex™ Substances 0.000 description 1
- 102000009843 Thyroglobulin Human genes 0.000 description 1
- 108010034949 Thyroglobulin Proteins 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 238000001261 affinity purification Methods 0.000 description 1
- 150000001299 aldehydes Chemical class 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000003638 chemical reducing agent Substances 0.000 description 1
- 238000011026 diafiltration Methods 0.000 description 1
- 150000002019 disulfides Chemical class 0.000 description 1
- 210000002889 endothelial cell Anatomy 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 238000002523 gelfiltration Methods 0.000 description 1
- 239000000710 homodimer Substances 0.000 description 1
- 229910052739 hydrogen Inorganic materials 0.000 description 1
- 239000001257 hydrogen Substances 0.000 description 1
- 125000004435 hydrogen atom Chemical class [H]* 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 238000002347 injection Methods 0.000 description 1
- 239000007924 injection Substances 0.000 description 1
- 210000003734 kidney Anatomy 0.000 description 1
- 239000002502 liposome Substances 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 239000000178 monomer Substances 0.000 description 1
- 108040007629 peroxidase activity proteins Proteins 0.000 description 1
- 230000004850 protein–protein interaction Effects 0.000 description 1
- 239000013014 purified material Substances 0.000 description 1
- 238000001542 size-exclusion chromatography Methods 0.000 description 1
- 210000000329 smooth muscle myocyte Anatomy 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 229960002175 thyroglobulin Drugs 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 210000004509 vascular smooth muscle cell Anatomy 0.000 description 1
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| SE0100625A SE0100625D0 (sv) | 2001-02-23 | 2001-02-23 | Methods for protein purification |
| US27224701P | 2001-02-28 | 2001-02-28 | |
| PCT/SE2002/000277 WO2002066669A1 (en) | 2001-02-23 | 2002-02-18 | Method for purification of soluble ssao |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JP2004520056A JP2004520056A (ja) | 2004-07-08 |
| JP2004520056A5 true JP2004520056A5 (enExample) | 2005-12-22 |
Family
ID=26655398
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2002566373A Pending JP2004520056A (ja) | 2001-02-23 | 2002-02-18 | 可溶性ｓｓａｏの精製のための方法 |
Country Status (6)
| Country | Link |
|---|---|
| US (1) | US20020160482A1 (enExample) |
| EP (1) | EP1362120A1 (enExample) |
| JP (1) | JP2004520056A (enExample) |
| CN (1) | CN1488000A (enExample) |
| CA (1) | CA2433408A1 (enExample) |
| WO (1) | WO2002066669A1 (enExample) |
Families Citing this family (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| AT502098B8 (de) * | 2004-07-07 | 2007-06-15 | Albert Dr Missbichler | Diaminooxidase-hältige zusammensetzung |
| WO2006103772A1 (ja) * | 2005-03-30 | 2006-10-05 | Nec Soft, Ltd. | グルタチオン－ｓ－トランスフェラーゼ・タンパク質に対する高親和性ｒｎａアプタマー分子 |
| RU2009130380A (ru) | 2007-01-10 | 2011-02-20 | Санофи-Авентис (Fr) | Способ определения стабильности органических метиленаминов в присутствии семикарбазид-чувствительной аминоксидазы |
| WO2010064748A1 (en) * | 2008-12-04 | 2010-06-10 | Korea Research Institute Of Bioscience And Biotechnology | Screening of abundantly secreted proteins and their use as fusion partners for the production of recombinant proteins |
| KR101291241B1 (ko) | 2010-11-04 | 2013-08-01 | 한국생명공학연구원 | 효모에서 인체 상피세포 성장인자를 대량 생산하는 방법 |
| US20140056870A1 (en) * | 2012-08-27 | 2014-02-27 | Allergan, Inc. | Fusion proteins |
Family Cites Families (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6100064A (en) * | 1984-04-06 | 2000-08-08 | Chiron Corporation | Secreted viral proteins useful for vaccines and diagnostics |
| CA2022713A1 (en) * | 1989-08-11 | 1991-02-12 | Nils U. Bang | Human thrombomodulin derivatives |
| AU4440496A (en) * | 1995-02-10 | 1996-08-22 | Smithkline Beecham Corporation | Use of src SH2 specific compounds to treat a bone resorption disease |
| CN1269829A (zh) * | 1997-05-23 | 2000-10-11 | 拜奥泰治疗有限公司 | 有胺氧化酶活性的血管粘着蛋白－1 |
-
2002
- 2002-02-18 EP EP02712575A patent/EP1362120A1/en not_active Withdrawn
- 2002-02-18 CN CNA028040066A patent/CN1488000A/zh active Pending
- 2002-02-18 CA CA002433408A patent/CA2433408A1/en not_active Abandoned
- 2002-02-18 WO PCT/SE2002/000277 patent/WO2002066669A1/en not_active Ceased
- 2002-02-18 JP JP2002566373A patent/JP2004520056A/ja active Pending
- 2002-02-21 US US10/081,408 patent/US20020160482A1/en not_active Abandoned
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