ES2253835T3 - Polipeptidos de cadena unica que contienen troponina i y troponina c. - Google Patents
Polipeptidos de cadena unica que contienen troponina i y troponina c.Info
- Publication number
- ES2253835T3 ES2253835T3 ES98958383T ES98958383T ES2253835T3 ES 2253835 T3 ES2253835 T3 ES 2253835T3 ES 98958383 T ES98958383 T ES 98958383T ES 98958383 T ES98958383 T ES 98958383T ES 2253835 T3 ES2253835 T3 ES 2253835T3
- Authority
- ES
- Spain
- Prior art keywords
- troponin
- sequence
- single chain
- polypeptide
- chain polypeptide
- 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
Links
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 88
- 229920001184 polypeptide Polymers 0.000 title claims abstract description 67
- 102000004196 processed proteins & peptides Human genes 0.000 title claims abstract description 67
- 108090000362 Lymphotoxin-beta Proteins 0.000 claims abstract description 60
- 102000013534 Troponin C Human genes 0.000 claims abstract description 60
- 238000003556 assay Methods 0.000 claims abstract description 23
- 102000013394 Troponin I Human genes 0.000 claims description 77
- 108010065729 Troponin I Proteins 0.000 claims description 77
- 230000000747 cardiac effect Effects 0.000 claims description 18
- 101710128251 Troponin I, cardiac muscle Proteins 0.000 claims description 6
- 102100036859 Troponin I, cardiac muscle Human genes 0.000 claims description 6
- 238000010367 cloning Methods 0.000 claims description 6
- 241000588724 Escherichia coli Species 0.000 claims description 5
- 239000013604 expression vector Substances 0.000 claims description 4
- 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 description 3
- 102000040430 polynucleotide Human genes 0.000 claims 5
- 108091033319 polynucleotide Proteins 0.000 claims 5
- 239000002157 polynucleotide Substances 0.000 claims 5
- 239000013599 cloning vector Substances 0.000 claims 1
- 108090001027 Troponin Proteins 0.000 abstract description 74
- 102000004903 Troponin Human genes 0.000 abstract description 73
- 238000002360 preparation method Methods 0.000 abstract description 20
- 230000002068 genetic effect Effects 0.000 abstract description 8
- 150000001413 amino acids Chemical class 0.000 abstract description 7
- 239000000427 antigen Substances 0.000 abstract description 6
- 102000036639 antigens Human genes 0.000 abstract description 6
- 108091007433 antigens Proteins 0.000 abstract description 6
- 101000851334 Homo sapiens Troponin I, cardiac muscle Proteins 0.000 abstract description 4
- 238000000746 purification Methods 0.000 abstract description 4
- 238000012360 testing method Methods 0.000 description 30
- 108091028043 Nucleic acid sequence Proteins 0.000 description 18
- 238000000034 method Methods 0.000 description 17
- 239000002299 complementary DNA Substances 0.000 description 13
- 210000004027 cell Anatomy 0.000 description 10
- 108020004705 Codon Proteins 0.000 description 8
- 125000003275 alpha amino acid group Chemical group 0.000 description 8
- 239000000463 material Substances 0.000 description 7
- 208000010125 myocardial infarction Diseases 0.000 description 7
- 210000004165 myocardium Anatomy 0.000 description 7
- 238000002405 diagnostic procedure Methods 0.000 description 6
- 102000004169 proteins and genes Human genes 0.000 description 6
- 108090000623 proteins and genes Proteins 0.000 description 6
- 102000001708 Protein Isoforms Human genes 0.000 description 5
- 108010029485 Protein Isoforms Proteins 0.000 description 5
- 230000001580 bacterial effect Effects 0.000 description 5
- 239000013612 plasmid Substances 0.000 description 5
- 230000035945 sensitivity Effects 0.000 description 5
- 210000002966 serum Anatomy 0.000 description 5
- 239000002773 nucleotide Substances 0.000 description 4
- 125000003729 nucleotide group Chemical group 0.000 description 4
- 238000000926 separation method Methods 0.000 description 4
- 210000002027 skeletal muscle Anatomy 0.000 description 4
- 230000008901 benefit Effects 0.000 description 3
- 210000004369 blood Anatomy 0.000 description 3
- 239000008280 blood Substances 0.000 description 3
- 238000010276 construction Methods 0.000 description 3
- 238000003745 diagnosis Methods 0.000 description 3
- 239000011159 matrix material Substances 0.000 description 3
- 238000005259 measurement Methods 0.000 description 3
- 230000002797 proteolythic effect Effects 0.000 description 3
- 238000010188 recombinant method Methods 0.000 description 3
- 241000894006 Bacteria Species 0.000 description 2
- TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 2
- 208000029549 Muscle injury Diseases 0.000 description 2
- 102000004987 Troponin T Human genes 0.000 description 2
- 108090001108 Troponin T Proteins 0.000 description 2
- 230000002159 abnormal effect Effects 0.000 description 2
- 210000001124 body fluid Anatomy 0.000 description 2
- 239000010839 body fluid Substances 0.000 description 2
- 238000006243 chemical reaction Methods 0.000 description 2
- CVSVTCORWBXHQV-UHFFFAOYSA-N creatine Chemical compound NC(=[NH2+])N(C)CC([O-])=O CVSVTCORWBXHQV-UHFFFAOYSA-N 0.000 description 2
- 230000001419 dependent effect Effects 0.000 description 2
- 238000011161 development Methods 0.000 description 2
- 238000010790 dilution Methods 0.000 description 2
- 239000012895 dilution Substances 0.000 description 2
- 238000010494 dissociation reaction Methods 0.000 description 2
- 230000005593 dissociations Effects 0.000 description 2
- 239000012634 fragment Substances 0.000 description 2
- 102000037865 fusion proteins Human genes 0.000 description 2
- 108020001507 fusion proteins Proteins 0.000 description 2
- 230000003993 interaction Effects 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 208000037891 myocardial injury Diseases 0.000 description 2
- 238000003752 polymerase chain reaction Methods 0.000 description 2
- 238000001742 protein purification Methods 0.000 description 2
- 230000000630 rising effect Effects 0.000 description 2
- 238000011896 sensitive detection Methods 0.000 description 2
- 239000000243 solution Substances 0.000 description 2
- 238000010561 standard procedure Methods 0.000 description 2
- 238000003860 storage Methods 0.000 description 2
- 108010030844 2-methylcitrate synthase Proteins 0.000 description 1
- JQDFGZKKXBEANU-IMJSIDKUSA-N Ala-Cys Chemical compound C[C@H](N)C(=O)N[C@@H](CS)C(O)=O JQDFGZKKXBEANU-IMJSIDKUSA-N 0.000 description 1
- 206010002383 Angina Pectoris Diseases 0.000 description 1
- 101100228196 Caenorhabditis elegans gly-4 gene Proteins 0.000 description 1
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 1
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 1
- 102000005701 Calcium-Binding Proteins Human genes 0.000 description 1
- 108010045403 Calcium-Binding Proteins Proteins 0.000 description 1
- 108010071536 Citrate (Si)-synthase Proteins 0.000 description 1
- 102000006732 Citrate synthase Human genes 0.000 description 1
- 108020004414 DNA Proteins 0.000 description 1
- 238000001712 DNA sequencing Methods 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 241001198387 Escherichia coli BL21(DE3) Species 0.000 description 1
- 241000287828 Gallus gallus Species 0.000 description 1
- 208000013875 Heart injury Diseases 0.000 description 1
- 101000764260 Homo sapiens Troponin T, cardiac muscle Proteins 0.000 description 1
- 102000013460 Malate Dehydrogenase Human genes 0.000 description 1
- 108010026217 Malate Dehydrogenase Proteins 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 102000008934 Muscle Proteins Human genes 0.000 description 1
- 108010074084 Muscle Proteins Proteins 0.000 description 1
- 102000036675 Myoglobin Human genes 0.000 description 1
- 108010062374 Myoglobin Proteins 0.000 description 1
- 125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 description 1
- 206010028851 Necrosis Diseases 0.000 description 1
- 206010062501 Non-cardiac chest pain Diseases 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 108091000080 Phosphotransferase Proteins 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- GXDLGHLJTHMDII-WISUUJSJSA-N Thr-Ser Chemical compound C[C@@H](O)[C@H](N)C(=O)N[C@@H](CO)C(O)=O GXDLGHLJTHMDII-WISUUJSJSA-N 0.000 description 1
- 102000005937 Tropomyosin Human genes 0.000 description 1
- 108010030743 Tropomyosin Proteins 0.000 description 1
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 1
- JAWMENYCRQKKJY-UHFFFAOYSA-N [3-(2,4,6,7-tetrahydrotriazolo[4,5-c]pyridin-5-ylmethyl)-1-oxa-2,8-diazaspiro[4.5]dec-2-en-8-yl]-[2-[[3-(trifluoromethoxy)phenyl]methylamino]pyrimidin-5-yl]methanone Chemical compound N1N=NC=2CN(CCC=21)CC1=NOC2(C1)CCN(CC2)C(=O)C=1C=NC(=NC=1)NCC1=CC(=CC=C1)OC(F)(F)F JAWMENYCRQKKJY-UHFFFAOYSA-N 0.000 description 1
- 230000001154 acute effect Effects 0.000 description 1
- 206010000891 acute myocardial infarction Diseases 0.000 description 1
- 230000001464 adherent effect Effects 0.000 description 1
- 230000004075 alteration Effects 0.000 description 1
- 239000012472 biological sample Substances 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 229910052791 calcium Inorganic materials 0.000 description 1
- 239000011575 calcium Substances 0.000 description 1
- 239000001110 calcium chloride Substances 0.000 description 1
- 229910001628 calcium chloride Inorganic materials 0.000 description 1
- 235000011148 calcium chloride Nutrition 0.000 description 1
- 239000004202 carbamide Substances 0.000 description 1
- 150000001718 carbodiimides Chemical class 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 150000001768 cations Chemical class 0.000 description 1
- 230000003196 chaotropic effect Effects 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 235000013330 chicken meat Nutrition 0.000 description 1
- 229960003624 creatine Drugs 0.000 description 1
- 239000006046 creatine Substances 0.000 description 1
- 238000004132 cross linking Methods 0.000 description 1
- 230000007812 deficiency Effects 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 201000006549 dyspepsia Diseases 0.000 description 1
- 238000013399 early diagnosis Methods 0.000 description 1
- 239000013613 expression plasmid Substances 0.000 description 1
- 239000012530 fluid Substances 0.000 description 1
- 230000004927 fusion Effects 0.000 description 1
- 230000004077 genetic alteration Effects 0.000 description 1
- 231100000118 genetic alteration Toxicity 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 210000005003 heart tissue Anatomy 0.000 description 1
- 102000050201 human TNNT2 Human genes 0.000 description 1
- 210000004408 hybridoma Anatomy 0.000 description 1
- 230000003053 immunization Effects 0.000 description 1
- 238000002649 immunization Methods 0.000 description 1
- 238000003018 immunoassay Methods 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 230000002401 inhibitory effect Effects 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 231100000518 lethal Toxicity 0.000 description 1
- 230000001665 lethal effect Effects 0.000 description 1
- 229910001629 magnesium chloride Inorganic materials 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 210000003205 muscle Anatomy 0.000 description 1
- 230000017074 necrotic cell death Effects 0.000 description 1
- 102000020233 phosphotransferase Human genes 0.000 description 1
- 210000002381 plasma Anatomy 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 230000017854 proteolysis Effects 0.000 description 1
- 230000006337 proteolytic cleavage Effects 0.000 description 1
- 238000003908 quality control method Methods 0.000 description 1
- 238000011002 quantification Methods 0.000 description 1
- 230000016150 regulation of muscle contraction Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 238000011895 specific detection Methods 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 238000010998 test method Methods 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 230000000451 tissue damage Effects 0.000 description 1
- 231100000827 tissue damage Toxicity 0.000 description 1
- 230000001131 transforming effect Effects 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
- C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
- C07K14/4702—Regulators; Modulating activity
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
- C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
- C07K14/4716—Muscle proteins, e.g. myosin, actin
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Zoology (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Gastroenterology & Hepatology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Toxicology (AREA)
- Peptides Or Proteins (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Investigating Or Analysing Biological Materials (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US993380 | 1992-12-18 | ||
| US08/993,380 US6077676A (en) | 1997-12-18 | 1997-12-18 | Single-chain polypeptides comprising troponin I and troponin C |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| ES2253835T3 true ES2253835T3 (es) | 2006-06-01 |
Family
ID=25539476
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| ES98958383T Expired - Lifetime ES2253835T3 (es) | 1997-12-18 | 1998-12-18 | Polipeptidos de cadena unica que contienen troponina i y troponina c. |
Country Status (9)
| Country | Link |
|---|---|
| US (1) | US6077676A (https=) |
| EP (1) | EP1037976B1 (https=) |
| JP (1) | JP4328019B2 (https=) |
| AT (1) | ATE309351T1 (https=) |
| AU (1) | AU1444699A (https=) |
| CA (1) | CA2315282C (https=) |
| DE (1) | DE69832299T2 (https=) |
| ES (1) | ES2253835T3 (https=) |
| WO (1) | WO1999031235A1 (https=) |
Families Citing this family (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| FR2756827B1 (fr) * | 1996-12-05 | 1999-01-29 | Pasteur Sanofi Diagnostics | Composes synthetiques biepitopiques utilisables comme etalons dans les dosages biologiques de la troponine i |
| US6475785B1 (en) * | 1997-12-18 | 2002-11-05 | Spectral Diagnostics, Inc. | Single-chain polypeptides comprising troponin I N-terminal fragments and troponin C |
| AU6117099A (en) | 1998-10-21 | 2000-05-08 | Spectral Diagnostics Inc. | Cardiac troponin i polypeptide fragments and uses in diagnostics |
| US7078486B2 (en) * | 1999-12-10 | 2006-07-18 | Spectral Diagnostics, Inc. | Single-chain polypeptides comprising troponin I and troponin C |
| US20070141710A1 (en) * | 2005-12-20 | 2007-06-21 | Beckman Coulter, Inc. | Stable calibrators for immunoassays |
| US20110306148A1 (en) | 2010-06-14 | 2011-12-15 | Siemens Healthcare Diagnostics Inc. | Composition for use as an assay reagent |
| CN107245103A (zh) * | 2016-12-30 | 2017-10-13 | 广西壮族自治区药用植物园 | 抗肿瘤重组蛋白ifti及其编码基因与应用 |
| CN107245102A (zh) * | 2016-12-30 | 2017-10-13 | 广西壮族自治区药用植物园 | 抗肿瘤重组蛋白gpti及其编码基因与应用 |
Family Cites Families (11)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4892827A (en) * | 1986-09-24 | 1990-01-09 | The United States Of America As Represented By The Department Of Health And Human Services | Recombinant pseudomonas exotoxins: construction of an active immunotoxin with low side effects |
| US5604105B1 (en) * | 1990-10-12 | 1999-08-24 | Spectral Diagnostics Inc | Method and device for diagnosingand distinguishing chest pain in early onset thereof |
| CA2027434C (en) * | 1990-10-12 | 1999-01-05 | George Jackowski | Diagnostic kit for diagnosing and distinguishing chest pain in early onset thereof |
| DE69334095T2 (de) * | 1992-07-17 | 2007-04-12 | Dana-Farber Cancer Institute, Boston | Verfahren zur intrazellulären Bindung von zielgerichteten Molekülen |
| FR2701954B1 (fr) * | 1993-02-23 | 1995-07-07 | Pasteur Sanofi Diagnostics | Composition stabilisée de troponine pour immunoessais et procédé de stabilisation de troponine pour immunoessais. |
| AU1274097A (en) * | 1995-11-29 | 1997-06-19 | Dade International Inc. | Human heart cnbr troponin i isoform and use of same |
| FI104857B (fi) * | 1996-01-15 | 2000-04-14 | Hytest Oy | Sydänlihaksen soluvaurioiden asteen mittaus immunokemiallisella menetelmällä sisältäen menetelmään soveliaat vasta-aineet |
| WO1997039132A1 (en) * | 1996-04-16 | 1997-10-23 | University Of Miami | Stabilized preparations of human troponins and modifications thereof, diagnostic assay methods and assay kits |
| EP0946198B1 (en) * | 1996-10-15 | 2002-06-19 | Medical Analysis Systems, Inc. | Method of stabilizing troponin I (cTnI) via conjugation with an active polymer |
| US5834210A (en) * | 1997-05-23 | 1998-11-10 | Spectral Diagnostics, Inc. | Stable troponin subunits and complexes |
| EP0983299A1 (en) * | 1997-05-29 | 2000-03-08 | Medical Analysis Systems, Inc. | Covalently coupled troponin complexes |
-
1997
- 1997-12-18 US US08/993,380 patent/US6077676A/en not_active Expired - Lifetime
-
1998
- 1998-12-18 EP EP98958383A patent/EP1037976B1/en not_active Expired - Lifetime
- 1998-12-18 AT AT98958383T patent/ATE309351T1/de not_active IP Right Cessation
- 1998-12-18 JP JP2000539135A patent/JP4328019B2/ja not_active Expired - Lifetime
- 1998-12-18 AU AU14446/99A patent/AU1444699A/en not_active Abandoned
- 1998-12-18 WO PCT/IB1998/002095 patent/WO1999031235A1/en not_active Ceased
- 1998-12-18 ES ES98958383T patent/ES2253835T3/es not_active Expired - Lifetime
- 1998-12-18 CA CA2315282A patent/CA2315282C/en not_active Expired - Lifetime
- 1998-12-18 DE DE69832299T patent/DE69832299T2/de not_active Expired - Lifetime
Also Published As
| Publication number | Publication date |
|---|---|
| WO1999031235A1 (en) | 1999-06-24 |
| DE69832299D1 (de) | 2005-12-15 |
| EP1037976A1 (en) | 2000-09-27 |
| DE69832299T2 (de) | 2006-08-10 |
| ATE309351T1 (de) | 2005-11-15 |
| EP1037976B1 (en) | 2005-11-09 |
| CA2315282C (en) | 2012-10-23 |
| CA2315282A1 (en) | 1999-06-24 |
| JP2002508181A (ja) | 2002-03-19 |
| US6077676A (en) | 2000-06-20 |
| JP4328019B2 (ja) | 2009-09-09 |
| AU1444699A (en) | 1999-07-05 |
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