DE69715641T2 - Reinigung von biologisch aktiven peptiden aus milch - Google Patents
Reinigung von biologisch aktiven peptiden aus milchInfo
- Publication number
- DE69715641T2 DE69715641T2 DE69715641T DE69715641T DE69715641T2 DE 69715641 T2 DE69715641 T2 DE 69715641T2 DE 69715641 T DE69715641 T DE 69715641T DE 69715641 T DE69715641 T DE 69715641T DE 69715641 T2 DE69715641 T2 DE 69715641T2
- Authority
- DE
- Germany
- Prior art keywords
- milk
- protein
- transgenic
- soluble
- component
- 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 - Lifetime
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- 241000700159 Rattus Species 0.000 description 1
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- 102000007562 Serum Albumin Human genes 0.000 description 1
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- 241000282898 Sus scrofa Species 0.000 description 1
- 101000712605 Theromyzon tessulatum Theromin Proteins 0.000 description 1
- 229940122388 Thrombin inhibitor Drugs 0.000 description 1
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- 150000007513 acids Chemical class 0.000 description 1
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- 230000008901 benefit Effects 0.000 description 1
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- OWMVSZAMULFTJU-UHFFFAOYSA-N bis-tris Chemical compound OCCN(CCO)C(CO)(CO)CO OWMVSZAMULFTJU-UHFFFAOYSA-N 0.000 description 1
- 229940019700 blood coagulation factors Drugs 0.000 description 1
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- 235000011850 desserts Nutrition 0.000 description 1
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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
- C07K1/36—Extraction; Separation; Purification by a combination of two or more processes of different types
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23J1/00—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites
- A23J1/20—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from milk, e.g. casein; from whey
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S530/00—Chemistry: natural resins or derivatives; peptides or proteins; lignins or reaction products thereof
- Y10S530/827—Proteins from mammals or birds
- Y10S530/832—Milk; colostrum
Landscapes
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Biochemistry (AREA)
- Organic Chemistry (AREA)
- Biophysics (AREA)
- Medicinal Chemistry (AREA)
- Analytical Chemistry (AREA)
- Health & Medical Sciences (AREA)
- Food Science & Technology (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Polymers & Plastics (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Engineering & Computer Science (AREA)
- Peptides Or Proteins (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US08/648,235 US6268487B1 (en) | 1996-05-13 | 1996-05-13 | Purification of biologically active peptides from milk |
| PCT/US1997/008044 WO1997042835A1 (en) | 1996-05-13 | 1997-05-13 | Purification of biologically active peptides from milk |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| DE69715641D1 DE69715641D1 (de) | 2002-10-24 |
| DE69715641T2 true DE69715641T2 (de) | 2003-08-07 |
Family
ID=24599969
Family Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| DE69715641T Expired - Lifetime DE69715641T2 (de) | 1996-05-13 | 1997-05-13 | Reinigung von biologisch aktiven peptiden aus milch |
| DE122007000008C Active DE122007000008I2 (de) | 1996-05-13 | 1997-05-13 | Reinigung von biologisch aktiven peptiden aus milch |
Family Applications After (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| DE122007000008C Active DE122007000008I2 (de) | 1996-05-13 | 1997-05-13 | Reinigung von biologisch aktiven peptiden aus milch |
Country Status (14)
| Country | Link |
|---|---|
| US (1) | US6268487B1 (enExample) |
| EP (1) | EP0923308B1 (enExample) |
| JP (1) | JP4476362B2 (enExample) |
| AT (1) | ATE224145T1 (enExample) |
| AU (1) | AU725993B2 (enExample) |
| CA (1) | CA2254871C (enExample) |
| DE (2) | DE69715641T2 (enExample) |
| DK (1) | DK0923308T3 (enExample) |
| ES (1) | ES2182074T3 (enExample) |
| LU (1) | LU91305I2 (enExample) |
| NL (1) | NL300256I2 (enExample) |
| NZ (1) | NZ332916A (enExample) |
| PT (1) | PT923308E (enExample) |
| WO (1) | WO1997042835A1 (enExample) |
Families Citing this family (71)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2874751B2 (ja) | 1986-04-09 | 1999-03-24 | ジェンザイム・コーポレーション | 希望する蛋白質をミルク中へ分泌する遺伝子移植動物 |
| CA2306796A1 (en) | 1997-10-20 | 1999-04-29 | Genzyme Transgenics Corporation | Novel modified msp-1 nucleic acid sequences and methods for increasing mrna levels and protein expression in cell systems |
| SE9802213D0 (sv) * | 1998-06-18 | 1998-06-18 | Amersham Pharm Biotech Ab | A method for the removal/purification of serum albumins and means for use in the method |
| US20030005468A1 (en) * | 1998-06-19 | 2003-01-02 | Meade Harry M. | Methods and vectors for improving nucleic acid expression |
| DE69931645T2 (de) * | 1998-09-24 | 2007-05-16 | Pharming Intellectual Property Bv | Reinigung von fibrinogen aus flüssigkeiten mittels ausfällung und hydrophobischer-interaktion-chromatographie |
| AU2492400A (en) * | 1999-01-06 | 2000-07-24 | Atlantic Biopharmaceuticals, Inc. | Expression of secreted human alpha-fetoprotein in transgenic animals |
| WO2001000855A1 (en) | 1999-06-23 | 2001-01-04 | Ppl Therapeutics (Scotland) Ltd. | Fusion proteins incorporating lysozyme |
| CN1431911A (zh) * | 2000-05-05 | 2003-07-23 | Gtc生物治疗学公司 | 转基因产生的核心蛋白聚糖 |
| US20030195707A1 (en) * | 2000-05-25 | 2003-10-16 | Schork Nicholas J | Methods of dna marker-based genetic analysis using estimated haplotype frequencies and uses thereof |
| US20020077775A1 (en) * | 2000-05-25 | 2002-06-20 | Schork Nicholas J. | Methods of DNA marker-based genetic analysis using estimated haplotype frequencies and uses thereof |
| US20040226052A1 (en) * | 2000-10-13 | 2004-11-11 | Meade Harry M. | Methods of producing a target molecule in a transgenic animal and purification of the target molecule |
| CA2448432A1 (en) * | 2001-06-13 | 2002-12-19 | Taurus Hsa Llc | Purification of human serum albumin |
| JP2005511012A (ja) * | 2001-08-10 | 2005-04-28 | セローノ ジェネティクス インスティテュート ソシエテ アノニム | ヒトcDNAおよびタンパク質およびその使用 |
| US6875459B2 (en) * | 2001-09-10 | 2005-04-05 | Henry B. Kopf | Method and apparatus for separation of milk, colostrum, and whey |
| US20060253913A1 (en) * | 2001-12-21 | 2006-11-09 | Yue-Jin Huang | Production of hSA-linked butyrylcholinesterases in transgenic mammals |
| WO2003090545A1 (en) * | 2002-04-24 | 2003-11-06 | Dairy Development Specialists, Inc. | Intermediate ingredient for dairy product manufacturing and method of making the same |
| EP1367065B1 (en) * | 2002-05-27 | 2008-07-30 | Nestec S.A. | Acid soluble proteins from micellar casein |
| GB0216001D0 (en) * | 2002-07-10 | 2002-08-21 | Nat Blood Authority | Process and composition |
| WO2004026427A2 (en) * | 2002-09-17 | 2004-04-01 | Gtc Biotherapeutics, Inc. | Isolation of immunoglobulin molecules that lack inter-heavy chain disulfide bonds |
| CA2506629A1 (en) * | 2002-11-27 | 2004-06-17 | Gtc Biotherapeutics, Inc. | Modified antibodies stably produced in milk and methods of producing same |
| US20040231010A1 (en) * | 2003-01-09 | 2004-11-18 | Murray James D. | Lysozyme transgenic ungulates |
| US20040210953A1 (en) * | 2003-01-09 | 2004-10-21 | Murray James D. | Lysozyme transgenic ungulates |
| US20040248262A1 (en) | 2003-01-22 | 2004-12-09 | Koeberl Dwight D. | Constructs for expressing lysomal polypeptides |
| CA2516836A1 (en) * | 2003-02-24 | 2004-09-10 | Gtc Biotherapeutics, Inc. | Methods of tangential flow filtration and an apparatus therefore |
| US7125963B2 (en) * | 2004-03-03 | 2006-10-24 | En N Tech Inc | Treatments for contaminant reduction in lactoferrin preparations and lactoferrin containing compositions |
| US20050197496A1 (en) * | 2004-03-04 | 2005-09-08 | Gtc Biotherapeutics, Inc. | Methods of protein fractionation using high performance tangential flow filtration |
| US20050245444A1 (en) * | 2004-04-30 | 2005-11-03 | Yann Echelard | Method of using recombinant human antithrombin for neurocognitive disorders |
| US20060121004A1 (en) * | 2004-12-07 | 2006-06-08 | Yann Echelard | Methods of reducing the incidence of rejection in tissue transplantation through the use of recombinant human antithrombin |
| US20060130159A1 (en) * | 2004-12-09 | 2006-06-15 | Nick Masiello | Method of purifying recombinant MSP 1-42 derived from Plasmodium falciparum |
| US20080019905A9 (en) * | 2005-02-18 | 2008-01-24 | Strome Scott E | Method of using an anti-CD137 antibody as an agent for radioimmunotherapy or radioimmunodetection |
| WO2006138647A2 (en) * | 2005-06-16 | 2006-12-28 | Gtc Biotherapeutics, Inc. | Method of making recombinant human antibodies for use in biosensor technology |
| WO2007014244A2 (en) * | 2005-07-25 | 2007-02-01 | Gtc Biotherapeutics, Inc. | Method of purifying recombinant human antithrombin to enhance the viral and prion safety profile |
| NZ568433A (en) * | 2005-10-21 | 2012-07-27 | Gtc Biotherapeutics Inc | Milk-derived antibodies with enhanced antibody-dependent cellular cytoxicity activity, methods of their production and use |
| US7531632B2 (en) * | 2006-02-16 | 2009-05-12 | Gtc Biotherapeutics, Inc. | Clarification of transgenic milk using depth filtration |
| FR2901707B1 (fr) | 2006-05-31 | 2017-09-29 | Lab Francais Du Fractionnement | Composition de facteur vii recombinant ou transgenique, chaque molecule de facteur vii possedant deux sites de n-glycosylation a motifs glycanniques definis |
| EP2049661A4 (en) * | 2006-08-04 | 2012-07-04 | Pharmathene Inc | RECOMBINANT BUTYRYLCHOLINESTERASE WITH LONG HALF-LIFE |
| FR2910786B1 (fr) * | 2006-12-29 | 2017-08-11 | Laboratoire Francais Du Fractionnement Et Des Biotechnologies (Lfb) | "procede d'extraction d'une proteine presente dans du lait" |
| JP5208428B2 (ja) * | 2007-01-30 | 2013-06-12 | 雪印メグミルク株式会社 | 美肌剤 |
| FR2912310B1 (fr) | 2007-02-13 | 2009-08-07 | Kasan Sarl | Nouvelles compositions cosmetiques et/ou pharmaceutiques et leurs applications. |
| NZ583234A (en) | 2007-07-10 | 2012-06-29 | Glanbia Nutritionals | Method for removing endotoxin from proteins |
| EP2077273B1 (en) | 2007-12-31 | 2011-09-14 | Animal Technology Institute Taiwan | Methods for separating casein from soluble proteins in a composition |
| TWI346666B (en) * | 2007-12-31 | 2011-08-11 | Animal Technology Inst Taiwan | Method for seperating casein from casein-contained solution |
| JP5447372B2 (ja) * | 2008-04-21 | 2014-03-19 | 不二製油株式会社 | 脱脂豆乳ペプチドの製造方法 |
| US20110229460A1 (en) * | 2008-05-01 | 2011-09-22 | Gtc Biotherapeutics, Inc. | anti-cd137 antibody as an agent in the treatment of inflammatory conditions |
| BRPI0911957A2 (pt) * | 2008-05-14 | 2016-08-23 | Agriculture Victoria Serv Pty | frações de leite enriquecidas com angiogenina |
| SG10201407983VA (en) * | 2009-12-18 | 2015-01-29 | Csl Ltd | Method of purifying polypeptides |
| WO2011084145A2 (en) | 2009-12-21 | 2011-07-14 | Pharmathene, Inc. | Recombinant butyrylcholinesterases and truncates thereof |
| US8861162B2 (en) * | 2010-03-09 | 2014-10-14 | Honeywell International Inc. | High power solid state power controller (SSPC) solution for primary power distribution applications |
| EP3175844A1 (en) | 2010-04-09 | 2017-06-07 | Pacira Pharmaceuticals, Inc. | Large diameter synthetic membrane vesicles |
| FR2958496A1 (fr) * | 2010-04-09 | 2011-10-14 | Bioprotein Technologies Sa | Preparation de proteine plasmatique de transfert des phospholipides (pltp) humaine recombinante a partir du lait d'animaux transgeniques. |
| US10138290B2 (en) | 2010-10-05 | 2018-11-27 | Novo Nordisk Healthcare Ag | Process for protein production |
| PH12013501365A1 (en) | 2010-12-30 | 2013-09-16 | Laboratoire Francais Du Fractionnment Et Des Biotechnologies | Glycols as pathogen inactivating agents |
| ES2886043T3 (es) | 2011-04-01 | 2021-12-16 | Emd Millipore Corp | Estructuras compuestas que contienen nanofibras |
| BR112014000217A2 (pt) * | 2011-07-07 | 2017-02-07 | Revo Biologics Inc | formulação e método para a criação de uma formulação que estabiliza a proteína terapêutica |
| TW201400499A (zh) | 2012-03-12 | 2014-01-01 | Revo Biolog Inc | 抗凝血酶用於治療妊娠毒血症之用途 |
| EP2687595B1 (en) | 2012-07-19 | 2018-05-30 | Laboratoire Français du Fractionnement et des Biotechnologies | Method for purifying transgenic factor VII |
| AR091977A1 (es) | 2012-08-03 | 2015-03-11 | Revo Biolog Inc | El uso de antitrombina en la oxigenacion de membranas extracorporeas |
| EP2956003A2 (en) | 2013-02-13 | 2015-12-23 | Laboratoire Français du Fractionnement et des Biotechnologies | Proteins with modified glycosylation and methods of production thereof |
| BR112015019341A2 (pt) | 2013-02-13 | 2017-08-22 | Lab Francais Du Fractionnement | Anticorpo anti-tnf-alfa, composição que compreende o anticorpo, método para produzir uma população de anticorpos, células epiteliais da glândula mamária, mamífero não humano transgênico, e, composição de anticorpo anti-tnf monoclonal |
| JP2016532100A (ja) | 2013-07-05 | 2016-10-13 | ラボラトワール・フランセ・デュ・フラクシオンマン・エ・デ・ビョテクノロジーLaboratoire Francais Du Fractionnement Et Des Biotechnologies | アフィニティークロマトグラフィーマトリックス |
| US9661868B2 (en) * | 2013-07-16 | 2017-05-30 | Mead Johnson Nutrition Company | Expanded bed adsorption methods for isolation of basic milk proteins including lactoferrin |
| US20170129966A1 (en) * | 2014-06-02 | 2017-05-11 | Laboratoire Français Du Fractionnement Et Des Biotechnologies | Production of fc fragments |
| ES2962695T3 (es) | 2014-06-26 | 2024-03-20 | Emd Millipore Corp | Dispositivo de filtración de fluidos con capacidad de retención de suciedad mejorada |
| FR3034419B1 (fr) | 2015-04-02 | 2017-12-15 | Lab Francais Du Fractionnement | Procede de purification d'une proteine recombinante therapeutique a partir d'un lait transgenique |
| WO2016167871A1 (en) | 2015-04-17 | 2016-10-20 | Emd Millipore Corporation | Method of purifying a biological materia of interest in a sample using nanofiber ultrafiltration membranes operated in tangential flow filtration mode |
| FR3038517B1 (fr) | 2015-07-06 | 2020-02-28 | Laboratoire Francais Du Fractionnement Et Des Biotechnologies | Utilisation de fragments fc modifies en immunotherapie |
| WO2019016605A1 (en) | 2017-07-21 | 2019-01-24 | Merck Millipore Ltd | MEMBRANES OF NONWOVEN FIBERS |
| WO2019223752A1 (zh) * | 2018-05-24 | 2019-11-28 | 江苏恒瑞医药股份有限公司 | 一种重组人胰岛素或其类似物的前体的制备方法 |
| FR3082427B1 (fr) | 2018-06-14 | 2020-09-25 | Lab Francais Du Fractionnement | Combinaison de facteur vii et d'un anticorps bispecifique anti-facteurs ix et x |
| JP7478333B2 (ja) * | 2020-07-29 | 2024-05-07 | 和弘 原 | 成分調整物生産装置及び成分調整物生産方法 |
| CN113101737B (zh) * | 2021-03-04 | 2023-09-15 | 京美生命科技(杭州)有限公司 | 一种亲和切向流过滤系统及其构建方法和外泌体提取方法及应用 |
Family Cites Families (17)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| FR2459619B1 (fr) | 1979-06-26 | 1983-07-29 | Agronomique Inst Nat Rech | Procede pour l'obtention a partir de lactoserum, d'un produit enrichi en alpha-lactalbumine et applications dudit procede |
| FR2487642B2 (fr) | 1980-07-31 | 1985-10-18 | Bel Fromageries | Procede de preparation de fractions proteiques par ultrafiltration et chromatographie d'exclusion et d'echange d'ions |
| DE3432718C1 (de) | 1984-09-06 | 1986-05-22 | Biotest Pharma GmbH, 6000 Frankfurt | Verfahren zur Herstellung einer Loesung von Milch- und/oder Kolostralimmunglobulinen |
| FR2584727B1 (fr) | 1985-07-11 | 1988-06-17 | Roussel Uclaf | Procede d'extraction de proteines du lait, produits, application du procede, et compositions pharmaceutiques |
| JPS62298536A (ja) | 1986-06-17 | 1987-12-25 | Green Cross Corp:The | 生理活性物質の自動精製方法および自動精製装置 |
| DE3743440A1 (de) * | 1987-12-21 | 1989-06-29 | Gauri Kailash Kumar | Verfahren zum trennen der geloesten und ungeloesten bestandteile von milch |
| US4897465A (en) | 1988-10-12 | 1990-01-30 | Abbott Laboratories | Enrichment and concentration of proteins by ultrafiltration |
| AU656720B2 (en) | 1989-12-01 | 1995-02-16 | Gene Pharming Europe Bv | Production of recombinant polypeptides by bovine species and transgenic methods |
| NL9001650A (nl) | 1990-07-19 | 1992-02-17 | Ver Coop Melkind | Werkwijze voor de bereiding van een melkeiwit-isolaat. |
| US5256294A (en) * | 1990-09-17 | 1993-10-26 | Genentech, Inc. | Tangential flow filtration process and apparatus |
| US5175013A (en) | 1990-12-31 | 1992-12-29 | The Pillsbury Company | Frozen dessert compositions and products |
| US5178894A (en) | 1991-09-26 | 1993-01-12 | Silvia P. Rudel | High non-fat milk content bread products having improved keeping qualities |
| JP3670003B2 (ja) | 1992-06-15 | 2005-07-13 | ファーミング ビー.ブイ. | ウシ種による組み換えポリペプチドの製造及びトランスジェニック法 |
| US5256437A (en) * | 1992-06-19 | 1993-10-26 | Pall Corporation | Product and process of making sterile milk through dynamic microfiltration |
| ATE193301T1 (de) | 1993-03-09 | 2000-06-15 | Genzyme Corp | Verfahren zur isolierung von proteinen aus milch |
| JPH09509165A (ja) | 1994-02-16 | 1997-09-16 | ファーミング ベスローテン フェンノートシャップ | ミルクからのラクトフェリンの分離 |
| US5597486A (en) * | 1995-05-01 | 1997-01-28 | Millipore Investment Holdings Limited | Membrane filtration with optimized addition of second liquid to maximize flux |
-
1996
- 1996-05-13 US US08/648,235 patent/US6268487B1/en not_active Expired - Lifetime
-
1997
- 1997-05-13 DE DE69715641T patent/DE69715641T2/de not_active Expired - Lifetime
- 1997-05-13 PT PT97923643T patent/PT923308E/pt unknown
- 1997-05-13 ES ES97923643T patent/ES2182074T3/es not_active Expired - Lifetime
- 1997-05-13 EP EP97923643A patent/EP0923308B1/en not_active Expired - Lifetime
- 1997-05-13 NZ NZ332916A patent/NZ332916A/xx not_active IP Right Cessation
- 1997-05-13 DE DE122007000008C patent/DE122007000008I2/de active Active
- 1997-05-13 JP JP54103697A patent/JP4476362B2/ja not_active Expired - Lifetime
- 1997-05-13 CA CA002254871A patent/CA2254871C/en not_active Expired - Lifetime
- 1997-05-13 AU AU29402/97A patent/AU725993B2/en not_active Expired
- 1997-05-13 WO PCT/US1997/008044 patent/WO1997042835A1/en not_active Ceased
- 1997-05-13 AT AT97923643T patent/ATE224145T1/de active
- 1997-05-13 DK DK97923643T patent/DK0923308T3/da active
-
2007
- 2007-01-12 LU LU91305C patent/LU91305I2/fr unknown
- 2007-01-19 NL NL300256C patent/NL300256I2/nl unknown
Also Published As
| Publication number | Publication date |
|---|---|
| EP0923308A1 (en) | 1999-06-23 |
| NZ332916A (en) | 2000-05-26 |
| NL300256I2 (nl) | 2007-09-03 |
| WO1997042835A1 (en) | 1997-11-20 |
| AU2940297A (en) | 1997-12-05 |
| DE69715641D1 (de) | 2002-10-24 |
| EP0923308A4 (enExample) | 1999-06-30 |
| JP2000510701A (ja) | 2000-08-22 |
| US6268487B1 (en) | 2001-07-31 |
| AU725993B2 (en) | 2000-10-26 |
| DE122007000008I1 (de) | 2009-05-20 |
| DE122007000008I2 (de) | 2011-01-13 |
| ATE224145T1 (de) | 2002-10-15 |
| NL300256I1 (nl) | 2007-04-02 |
| CA2254871A1 (en) | 1997-11-20 |
| CA2254871C (en) | 2008-03-25 |
| EP0923308B1 (en) | 2002-09-18 |
| PT923308E (pt) | 2002-11-29 |
| DK0923308T3 (da) | 2002-10-14 |
| JP4476362B2 (ja) | 2010-06-09 |
| LU91305I2 (fr) | 2007-03-12 |
| ES2182074T3 (es) | 2003-03-01 |
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