JP2006506613A5 - - Google Patents
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- JP2006506613A5 JP2006506613A5 JP2004551020A JP2004551020A JP2006506613A5 JP 2006506613 A5 JP2006506613 A5 JP 2006506613A5 JP 2004551020 A JP2004551020 A JP 2004551020A JP 2004551020 A JP2004551020 A JP 2004551020A JP 2006506613 A5 JP2006506613 A5 JP 2006506613A5
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- JP
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- Prior art keywords
- antibody
- pbs
- shows
- igg
- coli
- 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.)
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- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 49
- 239000002953 phosphate buffered saline Substances 0.000 description 49
- 210000004027 cell Anatomy 0.000 description 37
- 241000588724 Escherichia coli Species 0.000 description 29
- UJKPHYRXOLRVJJ-MLSVHJFASA-N CC(O)C1=C(C)/C2=C/C3=N/C(=C\C4=C(CCC(O)=O)C(C)=C(N4)/C=C4\N=C(\C=C\1/N\2)C(C)=C4C(C)O)/C(CCC(O)=O)=C3C Chemical compound CC(O)C1=C(C)/C2=C/C3=N/C(=C\C4=C(CCC(O)=O)C(C)=C(N4)/C=C4\N=C(\C=C\1/N\2)C(C)=C4C(C)O)/C(CCC(O)=O)=C3C UJKPHYRXOLRVJJ-MLSVHJFASA-N 0.000 description 22
- 238000003556 assay Methods 0.000 description 18
- 102000016938 Catalase Human genes 0.000 description 16
- 108010053835 Catalase Proteins 0.000 description 16
- 241000283073 Equus caballus Species 0.000 description 16
- 230000000694 effects Effects 0.000 description 16
- 238000000034 method Methods 0.000 description 15
- 230000015572 biosynthetic process Effects 0.000 description 13
- 210000000440 neutrophil Anatomy 0.000 description 12
- 241000699666 Mus <mouse, genus> Species 0.000 description 11
- 238000004519 manufacturing process Methods 0.000 description 11
- 238000001819 mass spectrum Methods 0.000 description 11
- 230000003647 oxidation Effects 0.000 description 11
- 238000007254 oxidation reaction Methods 0.000 description 11
- 230000000844 anti-bacterial effect Effects 0.000 description 10
- KHLVKKOJDHCJMG-QDBORUFSSA-L indigo carmine Chemical compound [Na+].[Na+].N/1C2=CC=C(S([O-])(=O)=O)C=C2C(=O)C\1=C1/NC2=CC=C(S(=O)(=O)[O-])C=C2C1=O KHLVKKOJDHCJMG-QDBORUFSSA-L 0.000 description 10
- 229960003988 indigo carmine Drugs 0.000 description 10
- 235000012738 indigotine Nutrition 0.000 description 10
- 239000004179 indigotine Substances 0.000 description 10
- QPBDAHXYPMQZTA-UHFFFAOYSA-N 2,3-dioxoindole-1-sulfonic acid Chemical compound C1=CC=C2N(S(=O)(=O)O)C(=O)C(=O)C2=C1 QPBDAHXYPMQZTA-UHFFFAOYSA-N 0.000 description 9
- 241001494479 Pecora Species 0.000 description 9
- 238000005259 measurement Methods 0.000 description 9
- PKYCWFICOKSIHZ-UHFFFAOYSA-N 1-(3,7-dihydroxyphenoxazin-10-yl)ethanone Chemical compound OC1=CC=C2N(C(=O)C)C3=CC=C(O)C=C3OC2=C1 PKYCWFICOKSIHZ-UHFFFAOYSA-N 0.000 description 8
- 229940126619 mouse monoclonal antibody Drugs 0.000 description 8
- 239000003642 reactive oxygen metabolite Substances 0.000 description 8
- 239000000427 antigen Substances 0.000 description 7
- 102000036639 antigens Human genes 0.000 description 7
- 108091007433 antigens Proteins 0.000 description 7
- 238000002474 experimental method Methods 0.000 description 7
- 239000000243 solution Substances 0.000 description 7
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 6
- 241000283973 Oryctolagus cuniculus Species 0.000 description 6
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 6
- WPYMKLBDIGXBTP-UHFFFAOYSA-N benzoic acid Chemical compound OC(=O)C1=CC=CC=C1 WPYMKLBDIGXBTP-UHFFFAOYSA-N 0.000 description 6
- ZFRKQXVRDFCRJG-UHFFFAOYSA-N skatole Chemical compound C1=CC=C2C(C)=CNC2=C1 ZFRKQXVRDFCRJG-UHFFFAOYSA-N 0.000 description 6
- 241000605059 Bacteroidetes Species 0.000 description 5
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 5
- 238000000502 dialysis Methods 0.000 description 5
- 239000000463 material Substances 0.000 description 5
- 239000000203 mixture Substances 0.000 description 5
- 239000001301 oxygen Substances 0.000 description 5
- 229910052760 oxygen Inorganic materials 0.000 description 5
- 108090000623 proteins and genes Proteins 0.000 description 5
- 230000004083 survival effect Effects 0.000 description 5
- 230000001580 bacterial effect Effects 0.000 description 4
- QWPPOHNGKGFGJK-UHFFFAOYSA-N hypochlorous acid Chemical compound ClO QWPPOHNGKGFGJK-UHFFFAOYSA-N 0.000 description 4
- 210000000265 leukocyte Anatomy 0.000 description 4
- 244000005700 microbiome Species 0.000 description 4
- 235000018102 proteins Nutrition 0.000 description 4
- 102000004169 proteins and genes Human genes 0.000 description 4
- 238000009281 ultraviolet germicidal irradiation Methods 0.000 description 4
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 3
- 239000005711 Benzoic acid Substances 0.000 description 3
- 108060003951 Immunoglobulin Proteins 0.000 description 3
- 241000699670 Mus sp. Species 0.000 description 3
- 108010058846 Ovalbumin Proteins 0.000 description 3
- CBENFWSGALASAD-UHFFFAOYSA-N Ozone Chemical compound [O-][O+]=O CBENFWSGALASAD-UHFFFAOYSA-N 0.000 description 3
- 235000010233 benzoic acid Nutrition 0.000 description 3
- 108010005774 beta-Galactosidase Proteins 0.000 description 3
- 230000001332 colony forming effect Effects 0.000 description 3
- PCHJSUWPFVWCPO-UHFFFAOYSA-N gold Chemical compound [Au] PCHJSUWPFVWCPO-UHFFFAOYSA-N 0.000 description 3
- 102000018358 immunoglobulin Human genes 0.000 description 3
- 208000015181 infectious disease Diseases 0.000 description 3
- 231100000225 lethality Toxicity 0.000 description 3
- 229940092253 ovalbumin Drugs 0.000 description 3
- 230000001590 oxidative effect Effects 0.000 description 3
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N silicon dioxide Inorganic materials O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 3
- 239000011780 sodium chloride Substances 0.000 description 3
- 230000001225 therapeutic effect Effects 0.000 description 3
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 3
- FHNFHKCVQCLJFQ-UHFFFAOYSA-N xenon atom Chemical compound [Xe] FHNFHKCVQCLJFQ-UHFFFAOYSA-N 0.000 description 3
- XKRFYHLGVUSROY-UHFFFAOYSA-N Argon Chemical compound [Ar] XKRFYHLGVUSROY-UHFFFAOYSA-N 0.000 description 2
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 2
- VEXZGXHMUGYJMC-UHFFFAOYSA-M Chloride anion Chemical compound [Cl-] VEXZGXHMUGYJMC-UHFFFAOYSA-M 0.000 description 2
- MYMOFIZGZYHOMD-UHFFFAOYSA-N Dioxygen Chemical compound O=O MYMOFIZGZYHOMD-UHFFFAOYSA-N 0.000 description 2
- 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
- 229910019093 NaOCl Inorganic materials 0.000 description 2
- CESGKXMBHGUQTB-VONOSFMSSA-N [(1S,2S,6R,10S,11R,13S,14R,15R)-1,6,14-trihydroxy-8-(hydroxymethyl)-4,12,12,15-tetramethyl-5-oxo-13-tetracyclo[8.5.0.02,6.011,13]pentadeca-3,8-dienyl] tetradecanoate Chemical compound C1=C(CO)C[C@]2(O)C(=O)C(C)=C[C@H]2[C@@]2(O)[C@H](C)[C@@H](O)[C@@]3(OC(=O)CCCCCCCCCCCCC)C(C)(C)[C@H]3[C@@H]21 CESGKXMBHGUQTB-VONOSFMSSA-N 0.000 description 2
- 239000004480 active ingredient Substances 0.000 description 2
- WQZGKKKJIJFFOK-FPRJBGLDSA-N beta-D-galactose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@H]1O WQZGKKKJIJFFOK-FPRJBGLDSA-N 0.000 description 2
- 210000004369 blood Anatomy 0.000 description 2
- 239000008280 blood Substances 0.000 description 2
- 210000001772 blood platelet Anatomy 0.000 description 2
- 229940098773 bovine serum albumin Drugs 0.000 description 2
- 239000003054 catalyst Substances 0.000 description 2
- 238000006243 chemical reaction Methods 0.000 description 2
- 239000013078 crystal Substances 0.000 description 2
- 230000001419 dependent effect Effects 0.000 description 2
- 238000000635 electron micrograph Methods 0.000 description 2
- 230000007613 environmental effect Effects 0.000 description 2
- 210000003743 erythrocyte Anatomy 0.000 description 2
- 238000001914 filtration Methods 0.000 description 2
- 239000012634 fragment Substances 0.000 description 2
- 239000010931 gold Substances 0.000 description 2
- 229910052737 gold Inorganic materials 0.000 description 2
- 229960003569 hematoporphyrin Drugs 0.000 description 2
- 230000028993 immune response Effects 0.000 description 2
- 230000002458 infectious effect Effects 0.000 description 2
- 230000028709 inflammatory response Effects 0.000 description 2
- 230000005764 inhibitory process Effects 0.000 description 2
- 238000002347 injection Methods 0.000 description 2
- 239000007924 injection Substances 0.000 description 2
- 210000004698 lymphocyte Anatomy 0.000 description 2
- 239000007800 oxidant agent Substances 0.000 description 2
- 238000002360 preparation method Methods 0.000 description 2
- 239000010453 quartz Substances 0.000 description 2
- SUKJFIGYRHOWBL-UHFFFAOYSA-N sodium hypochlorite Chemical compound [Na+].Cl[O-] SUKJFIGYRHOWBL-UHFFFAOYSA-N 0.000 description 2
- 238000001228 spectrum Methods 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- 230000007704 transition Effects 0.000 description 2
- 229910052724 xenon Inorganic materials 0.000 description 2
- 102100026189 Beta-galactosidase Human genes 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- 101000609762 Gallus gallus Ovalbumin Proteins 0.000 description 1
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 1
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 1
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 1
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 1
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 1
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 1
- 102000004407 Lactalbumin Human genes 0.000 description 1
- 108090000942 Lactalbumin Proteins 0.000 description 1
- OUUQCZGPVNCOIJ-UHFFFAOYSA-M Superoxide Chemical compound [O-][O] OUUQCZGPVNCOIJ-UHFFFAOYSA-M 0.000 description 1
- 102000019197 Superoxide Dismutase Human genes 0.000 description 1
- 108010012715 Superoxide dismutase Proteins 0.000 description 1
- 101710120037 Toxin CcdB Proteins 0.000 description 1
- 239000007983 Tris buffer Substances 0.000 description 1
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 1
- 238000000862 absorption spectrum Methods 0.000 description 1
- 238000001720 action spectrum Methods 0.000 description 1
- 238000012870 ammonium sulfate precipitation Methods 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 150000001450 anions Chemical class 0.000 description 1
- 229910052786 argon Inorganic materials 0.000 description 1
- 239000011324 bead Substances 0.000 description 1
- 210000001185 bone marrow Anatomy 0.000 description 1
- 239000000872 buffer Substances 0.000 description 1
- 210000000170 cell membrane Anatomy 0.000 description 1
- 210000000991 chicken egg Anatomy 0.000 description 1
- 230000001086 cytosolic effect Effects 0.000 description 1
- 238000013480 data collection Methods 0.000 description 1
- 230000000850 deacetylating effect Effects 0.000 description 1
- 238000007872 degassing Methods 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- 238000000132 electrospray ionisation Methods 0.000 description 1
- 238000010828 elution Methods 0.000 description 1
- 230000005284 excitation Effects 0.000 description 1
- 230000007717 exclusion Effects 0.000 description 1
- 238000002073 fluorescence micrograph Methods 0.000 description 1
- 238000009472 formulation Methods 0.000 description 1
- 230000004927 fusion Effects 0.000 description 1
- 210000000777 hematopoietic system Anatomy 0.000 description 1
- 210000000987 immune system Anatomy 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 230000002401 inhibitory effect Effects 0.000 description 1
- 238000002372 labelling Methods 0.000 description 1
- 238000012417 linear regression Methods 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 238000005949 ozonolysis reaction Methods 0.000 description 1
- 229940097156 peroxyl Drugs 0.000 description 1
- 210000001539 phagocyte Anatomy 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 229920001184 polypeptide Polymers 0.000 description 1
- 108090000765 processed proteins & peptides Proteins 0.000 description 1
- 102000004196 processed proteins & peptides Human genes 0.000 description 1
- 230000002035 prolonged effect Effects 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 150000003254 radicals Chemical class 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 239000001488 sodium phosphate Substances 0.000 description 1
- 229910000162 sodium phosphate Inorganic materials 0.000 description 1
- 231100000419 toxicity Toxicity 0.000 description 1
- 230000001988 toxicity Effects 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 1
- 125000000430 tryptophan group Chemical group [H]N([H])C(C(=O)O*)C([H])([H])C1=C([H])N([H])C2=C([H])C([H])=C([H])C([H])=C12 0.000 description 1
- 230000035899 viability Effects 0.000 description 1
- 235000021241 α-lactalbumin Nutrition 0.000 description 1
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US42624502P | 2002-11-14 | 2002-11-14 | |
| PCT/EP2003/012710 WO2004044582A2 (en) | 2002-11-14 | 2003-11-13 | Antibody- or neutrophil-mediated ozone generation |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JP2006506613A JP2006506613A (ja) | 2006-02-23 |
| JP2006506613A5 true JP2006506613A5 (enExample) | 2006-12-28 |
Family
ID=32313124
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2004551020A Pending JP2006506613A (ja) | 2002-11-14 | 2003-11-13 | 抗体または好中球を介するオゾン生成 |
Country Status (8)
| Country | Link |
|---|---|
| US (1) | US20060292076A1 (enExample) |
| EP (1) | EP1563299A2 (enExample) |
| JP (1) | JP2006506613A (enExample) |
| CN (1) | CN100570365C (enExample) |
| AU (1) | AU2003288058A1 (enExample) |
| BR (1) | BR0315628A (enExample) |
| CA (1) | CA2505923A1 (enExample) |
| WO (1) | WO2004044582A2 (enExample) |
Families Citing this family (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP4998230B2 (ja) * | 2007-11-26 | 2012-08-15 | 株式会社島津製作所 | タンパク質試料中のメチオニン残基の酸化状態を解析する方法 |
Family Cites Families (22)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4684521A (en) * | 1982-12-08 | 1987-08-04 | Frederic A. Bourke, Jr. | Method and system for externally treating the blood |
| US4559157A (en) * | 1983-04-21 | 1985-12-17 | Creative Products Resource Associates, Ltd. | Cosmetic applicator useful for skin moisturizing |
| LU84979A1 (fr) * | 1983-08-30 | 1985-04-24 | Oreal | Composition cosmetique ou pharmaceutique sous forme aqueuse ou anhydre dont la phase grasse contient un polyether oligomere et polyethers oligomeres nouveaux |
| US5162217A (en) * | 1984-08-27 | 1992-11-10 | Bio-Technology General Corp. | Plasmids for expression of human superoxide dismutase (SOD) analogs containing lambda PL promoter with engineered restriction site for substituting ribosomal binding sites and methods of use thereof |
| US6030611A (en) * | 1984-08-27 | 2000-02-29 | Bio-Technology General Corp. | Therapeutic SOD compositions and uses thereof |
| US5248603A (en) * | 1985-09-03 | 1993-09-28 | Symbicom Aktiebolag | Superoxide dismutase |
| DE3619436A1 (de) * | 1986-06-10 | 1987-12-17 | Bayer Ag | Triaryl- und trihetarylmethanderivate als redoxindikatoren und deren verwendung |
| US4820508A (en) * | 1987-06-23 | 1989-04-11 | Neutrogena Corporation | Skin protective composition |
| US4992478A (en) * | 1988-04-04 | 1991-02-12 | Warner-Lambert Company | Antiinflammatory skin moisturizing composition and method of preparing same |
| DE4038563A1 (de) * | 1990-12-04 | 1992-06-11 | Gruenenthal Gmbh | Verwendung von superoxiddismutasen zur prophylaxe und/oder behandlung von organversagen bei risikopatienten mit polytrauma |
| US5807884A (en) * | 1992-10-30 | 1998-09-15 | Emory University | Treatment for atherosclerosis and other cardiovascular and inflammatory diseases |
| US5637315A (en) * | 1993-01-04 | 1997-06-10 | Thomas Jefferson University | Treatment of disease states induced by oxidative stress |
| US5747026A (en) * | 1993-10-15 | 1998-05-05 | University Of Alabama At Birmingham Research Foundation | Antioxidants |
| US5599712A (en) * | 1993-10-15 | 1997-02-04 | University Of Pittsburgh | Protection from ionizing irradiation or chemotherapeutic drug damage by in vivo gene therapy |
| US5647315A (en) * | 1994-10-07 | 1997-07-15 | Yamaha Hatsudoki Kabushiki Kaisha | Lubricating arrangement for engine |
| JPH08249306A (ja) * | 1995-03-09 | 1996-09-27 | Sharp Corp | データ駆動型情報処理装置 |
| US6822070B2 (en) * | 1996-03-11 | 2004-11-23 | David Baltimore | Truncated CRAF1 inhibits CD40 signaling |
| AU2394597A (en) * | 1996-04-18 | 1997-11-07 | Medical Research Council | Oxidative metabolism in smooth muscle cells: methods and materials relating thereto |
| GB9621440D0 (en) * | 1996-10-15 | 1996-12-04 | Renold Plc | A chain tensioner |
| GB9622159D0 (en) * | 1996-10-24 | 1996-12-18 | Solvay Sociutu Anonyme | Polyanionic polymers as adjuvants for mucosal immunization |
| US6040611A (en) * | 1998-09-10 | 2000-03-21 | Hughes Electonics Corporation | Microelectromechanical device |
| EP1153010A1 (en) * | 1999-02-08 | 2001-11-14 | Checkpoint Genetics, Inc. | $i(N)-SUBSTITUTED AMINO ACIDS, ANTIOXIDANT PHARMACEUTICAL COMPOSITIONS CONTAINING SAME AND METHODS USING SAME |
-
2003
- 2003-11-13 JP JP2004551020A patent/JP2006506613A/ja active Pending
- 2003-11-13 EP EP03779920A patent/EP1563299A2/en not_active Withdrawn
- 2003-11-13 WO PCT/EP2003/012710 patent/WO2004044582A2/en not_active Ceased
- 2003-11-13 AU AU2003288058A patent/AU2003288058A1/en not_active Abandoned
- 2003-11-13 CN CNB2003801087252A patent/CN100570365C/zh not_active Expired - Fee Related
- 2003-11-13 CA CA002505923A patent/CA2505923A1/en not_active Abandoned
- 2003-11-13 US US10/534,574 patent/US20060292076A1/en not_active Abandoned
- 2003-11-13 BR BR0315628-1A patent/BR0315628A/pt not_active IP Right Cessation
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