CA2545458A1 - Preparation seche de alpha 1-antitrypsine humaine obtenue par recombinaison - Google Patents
Preparation seche de alpha 1-antitrypsine humaine obtenue par recombinaison Download PDFInfo
- Publication number
- CA2545458A1 CA2545458A1 CA002545458A CA2545458A CA2545458A1 CA 2545458 A1 CA2545458 A1 CA 2545458A1 CA 002545458 A CA002545458 A CA 002545458A CA 2545458 A CA2545458 A CA 2545458A CA 2545458 A1 CA2545458 A1 CA 2545458A1
- Authority
- CA
- Canada
- Prior art keywords
- dry powder
- powder composition
- raat
- less
- protein content
- 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.)
- Abandoned
Links
- 239000000203 mixture Substances 0.000 title claims abstract description 83
- 101000823116 Homo sapiens Alpha-1-antitrypsin Proteins 0.000 title claims abstract 3
- 102000051631 human SERPINA1 Human genes 0.000 title claims abstract 3
- 238000009472 formulation Methods 0.000 title description 47
- 239000000843 powder Substances 0.000 claims abstract description 30
- 150000003839 salts Chemical class 0.000 claims description 17
- 230000000694 effects Effects 0.000 claims description 14
- 235000000346 sugar Nutrition 0.000 claims description 12
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 9
- KRKNYBCHXYNGOX-UHFFFAOYSA-K Citrate Chemical compound [O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O KRKNYBCHXYNGOX-UHFFFAOYSA-K 0.000 claims description 7
- PWKSKIMOESPYIA-BYPYZUCNSA-N L-N-acetyl-Cysteine Chemical compound CC(=O)N[C@@H](CS)C(O)=O PWKSKIMOESPYIA-BYPYZUCNSA-N 0.000 claims description 6
- 229960004308 acetylcysteine Drugs 0.000 claims description 6
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 claims description 5
- 239000000872 buffer Substances 0.000 claims description 5
- 239000000178 monomer Substances 0.000 claims description 5
- 239000004094 surface-active agent Substances 0.000 claims description 5
- CIWBSHSKHKDKBQ-JLAZNSOCSA-N Ascorbic acid Chemical compound OC[C@H](O)[C@H]1OC(=O)C(O)=C1O CIWBSHSKHKDKBQ-JLAZNSOCSA-N 0.000 claims description 4
- RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 claims description 4
- 229920001214 Polysorbate 60 Polymers 0.000 claims description 3
- 239000003963 antioxidant agent Substances 0.000 claims description 3
- 235000006708 antioxidants Nutrition 0.000 claims description 3
- 239000002738 chelating agent Substances 0.000 claims description 3
- 239000003638 chemical reducing agent Substances 0.000 claims description 3
- 102000009027 Albumins Human genes 0.000 claims description 2
- 108010088751 Albumins Proteins 0.000 claims 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 claims description 2
- 108010024636 Glutathione Proteins 0.000 claims description 2
- 102000003839 Human Proteins Human genes 0.000 claims description 2
- 108090000144 Human Proteins Proteins 0.000 claims description 2
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 claims description 2
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 claims description 2
- 229910019142 PO4 Inorganic materials 0.000 claims description 2
- 229960005070 ascorbic acid Drugs 0.000 claims description 2
- 235000010323 ascorbic acid Nutrition 0.000 claims description 2
- 239000011668 ascorbic acid Substances 0.000 claims description 2
- 239000003541 chymotrypsin inhibitor Substances 0.000 claims description 2
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 claims description 2
- 235000018417 cysteine Nutrition 0.000 claims description 2
- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 claims description 2
- 229960003180 glutathione Drugs 0.000 claims description 2
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 claims description 2
- 230000002779 inactivation Effects 0.000 claims description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 claims description 2
- 239000010452 phosphate Substances 0.000 claims description 2
- 230000003612 virological effect Effects 0.000 claims description 2
- FFEARJCKVFRZRR-UHFFFAOYSA-N L-Methionine Natural products CSCCC(N)C(O)=O FFEARJCKVFRZRR-UHFFFAOYSA-N 0.000 claims 1
- 229930195722 L-methionine Natural products 0.000 claims 1
- NWGKJDSIEKMTRX-AAZCQSIUSA-N Sorbitan monooleate Chemical compound CCCCCCCC\C=C/CCCCCCCC(=O)OC[C@@H](O)[C@H]1OC[C@H](O)[C@H]1O NWGKJDSIEKMTRX-AAZCQSIUSA-N 0.000 claims 1
- 230000003078 antioxidant effect Effects 0.000 claims 1
- 229960004452 methionine Drugs 0.000 claims 1
- 229950004959 sorbitan oleate Drugs 0.000 claims 1
- 102000004169 proteins and genes Human genes 0.000 description 16
- 108090000623 proteins and genes Proteins 0.000 description 16
- 235000018102 proteins Nutrition 0.000 description 15
- 102000015395 alpha 1-Antitrypsin Human genes 0.000 description 12
- 108010050122 alpha 1-Antitrypsin Proteins 0.000 description 12
- 229940024142 alpha 1-antitrypsin Drugs 0.000 description 11
- 239000007788 liquid Substances 0.000 description 10
- 238000004108 freeze drying Methods 0.000 description 9
- 238000005033 Fourier transform infrared spectroscopy Methods 0.000 description 8
- 238000001035 drying Methods 0.000 description 7
- 238000000034 method Methods 0.000 description 6
- 239000007787 solid Substances 0.000 description 5
- 150000008163 sugars Chemical class 0.000 description 5
- 239000000546 pharmaceutical excipient Substances 0.000 description 4
- 238000001694 spray drying Methods 0.000 description 4
- 150000001413 amino acids Chemical class 0.000 description 3
- 238000003556 assay Methods 0.000 description 3
- 235000010482 polyoxyethylene sorbitan monooleate Nutrition 0.000 description 3
- 229920000053 polysorbate 80 Polymers 0.000 description 3
- 239000001488 sodium phosphate Substances 0.000 description 3
- 229910000162 sodium phosphate Inorganic materials 0.000 description 3
- 230000003595 spectral effect Effects 0.000 description 3
- 239000007921 spray Substances 0.000 description 3
- 230000006641 stabilisation Effects 0.000 description 3
- 238000011105 stabilization Methods 0.000 description 3
- 239000003381 stabilizer Substances 0.000 description 3
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 3
- 238000001157 Fourier transform infrared spectrum Methods 0.000 description 2
- 150000001408 amides Chemical class 0.000 description 2
- 235000001014 amino acid Nutrition 0.000 description 2
- 230000015572 biosynthetic process Effects 0.000 description 2
- 238000004925 denaturation Methods 0.000 description 2
- 230000036425 denaturation Effects 0.000 description 2
- 230000009477 glass transition Effects 0.000 description 2
- 238000010438 heat treatment Methods 0.000 description 2
- 239000012931 lyophilized formulation Substances 0.000 description 2
- 230000014759 maintenance of location Effects 0.000 description 2
- 239000002245 particle Substances 0.000 description 2
- 238000005057 refrigeration Methods 0.000 description 2
- 230000000717 retained effect Effects 0.000 description 2
- 238000001542 size-exclusion chromatography Methods 0.000 description 2
- JHJLBTNAGRQEKS-UHFFFAOYSA-M sodium bromide Chemical compound [Na+].[Br-] JHJLBTNAGRQEKS-UHFFFAOYSA-M 0.000 description 2
- HDTRYLNUVZCQOY-UHFFFAOYSA-N α-D-glucopyranosyl-α-D-glucopyranoside Natural products OC1C(O)C(O)C(CO)OC1OC1C(O)C(O)C(O)C(CO)O1 HDTRYLNUVZCQOY-UHFFFAOYSA-N 0.000 description 1
- 102000004506 Blood Proteins Human genes 0.000 description 1
- 108010017384 Blood Proteins Proteins 0.000 description 1
- XUYPXLNMDZIRQH-LURJTMIESA-N N-acetyl-L-methionine Chemical group CSCC[C@@H](C(O)=O)NC(C)=O XUYPXLNMDZIRQH-LURJTMIESA-N 0.000 description 1
- 102000016387 Pancreatic elastase Human genes 0.000 description 1
- 108010067372 Pancreatic elastase Proteins 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 1
- 229930006000 Sucrose Natural products 0.000 description 1
- HDTRYLNUVZCQOY-WSWWMNSNSA-N Trehalose Natural products O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@H](O)[C@@H](O)[C@@H](O)[C@@H](CO)O1 HDTRYLNUVZCQOY-WSWWMNSNSA-N 0.000 description 1
- 230000001154 acute effect Effects 0.000 description 1
- 238000012387 aerosolization Methods 0.000 description 1
- HDTRYLNUVZCQOY-LIZSDCNHSA-N alpha,alpha-trehalose Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 HDTRYLNUVZCQOY-LIZSDCNHSA-N 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 150000001450 anions Chemical class 0.000 description 1
- 239000004067 bulking agent Substances 0.000 description 1
- 150000001768 cations Chemical class 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- 239000000470 constituent Substances 0.000 description 1
- 229960002433 cysteine Drugs 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 239000000428 dust Substances 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 238000001704 evaporation Methods 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 239000012530 fluid Substances 0.000 description 1
- 230000005714 functional activity Effects 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- 230000036571 hydration Effects 0.000 description 1
- 238000006703 hydration reaction Methods 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 238000001990 intravenous administration Methods 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 229920001223 polyethylene glycol Polymers 0.000 description 1
- 239000000244 polyoxyethylene sorbitan monooleate Substances 0.000 description 1
- 229920000136 polysorbate Polymers 0.000 description 1
- 229940068968 polysorbate 80 Drugs 0.000 description 1
- 229940124606 potential therapeutic agent Drugs 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 108090000765 processed proteins & peptides Proteins 0.000 description 1
- 229940099982 prolastin Drugs 0.000 description 1
- 230000002685 pulmonary effect Effects 0.000 description 1
- 238000003998 size exclusion chromatography high performance liquid chromatography Methods 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 238000001179 sorption measurement Methods 0.000 description 1
- 238000001228 spectrum Methods 0.000 description 1
- 230000000087 stabilizing effect Effects 0.000 description 1
- 239000008223 sterile water Substances 0.000 description 1
- 238000007920 subcutaneous administration Methods 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000005720 sucrose Substances 0.000 description 1
- 230000008646 thermal stress Effects 0.000 description 1
- 230000000699 topical effect Effects 0.000 description 1
- 239000002753 trypsin inhibitor Substances 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
- C07K14/81—Protease inhibitors
- C07K14/8107—Endopeptidase (E.C. 3.4.21-99) inhibitors
- C07K14/811—Serine protease (E.C. 3.4.21) inhibitors
- C07K14/8121—Serpins
- C07K14/8125—Alpha-1-antitrypsin
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/55—Protease inhibitors
- A61K38/57—Protease inhibitors from animals; from humans
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K9/00—Medicinal preparations characterised by special physical form
- A61K9/14—Particulate form, e.g. powders, Processes for size reducing of pure drugs or the resulting products, Pure drug nanoparticles
- A61K9/16—Agglomerates; Granulates; Microbeadlets ; Microspheres; Pellets; Solid products obtained by spray drying, spray freeze drying, spray congealing,(multiple) emulsion solvent evaporation or extraction
- A61K9/1605—Excipients; Inactive ingredients
- A61K9/1611—Inorganic compounds
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K9/00—Medicinal preparations characterised by special physical form
- A61K9/14—Particulate form, e.g. powders, Processes for size reducing of pure drugs or the resulting products, Pure drug nanoparticles
- A61K9/19—Particulate form, e.g. powders, Processes for size reducing of pure drugs or the resulting products, Pure drug nanoparticles lyophilised, i.e. freeze-dried, solutions or dispersions
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Engineering & Computer Science (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Epidemiology (AREA)
- Organic Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Gastroenterology & Hepatology (AREA)
- Zoology (AREA)
- Inorganic Chemistry (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Genetics & Genomics (AREA)
- Molecular Biology (AREA)
- Immunology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicinal Preparation (AREA)
Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US51880303P | 2003-11-10 | 2003-11-10 | |
| US60/518,803 | 2003-11-10 | ||
| US51994603P | 2003-11-14 | 2003-11-14 | |
| US60/519,946 | 2003-11-14 | ||
| PCT/GB2004/004740 WO2005047323A1 (fr) | 2003-11-10 | 2004-11-10 | Preparation seche de alpha 1-antitrypsine humaine obtenue par recombinaison |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA2545458A1 true CA2545458A1 (fr) | 2005-05-26 |
Family
ID=34594925
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA002545458A Abandoned CA2545458A1 (fr) | 2003-11-10 | 2004-11-10 | Preparation seche de alpha 1-antitrypsine humaine obtenue par recombinaison |
Country Status (5)
| Country | Link |
|---|---|
| EP (1) | EP1685160A1 (fr) |
| JP (1) | JP2007534633A (fr) |
| AU (1) | AU2004288854B2 (fr) |
| CA (1) | CA2545458A1 (fr) |
| WO (1) | WO2005047323A1 (fr) |
Families Citing this family (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2007511539A (ja) * | 2003-11-14 | 2007-05-10 | バクスター・インターナショナル・インコーポレイテッド | α１−抗トリプシン組成物およびこのような組成物を用いた処置方法 |
| GB0710529D0 (en) | 2007-06-01 | 2007-07-11 | Circassia Ltd | Vaccine |
| MX2010001779A (es) | 2007-08-15 | 2010-07-06 | Circassia Ltd | Peptidos para vacunas. |
| HUE030205T2 (en) * | 2007-11-02 | 2017-05-29 | Grifols Therapeutics Inc | A method, composition, and product for providing alpha-1-antitrypsin |
| GB0821806D0 (en) | 2008-11-28 | 2009-01-07 | Circassia Ltd | Compositions with reduced dimer formation |
| WO2010112547A1 (fr) * | 2009-03-31 | 2010-10-07 | Gambro Lundia Ab | Composition précurseur de dialyse |
| US9353165B2 (en) | 2012-07-25 | 2016-05-31 | Grifols, S.A. | Purification of cell culture derived alpha1 protease inhibitor |
| MX375448B (es) * | 2013-07-18 | 2025-03-06 | Mannkind Corp | Composiciones farmacéuticas en polvo seco estables al calor y métodos. |
| IL267923B2 (en) * | 2018-08-02 | 2023-06-01 | Grifols Worldwide Operations Ltd | The composition containing the most concentrated alpha-1 type protein inhibitor and a method for obtaining it |
Family Cites Families (16)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| AU577259B2 (en) * | 1982-08-13 | 1988-09-22 | Zymogenetics Inc. | Glycolytic promters for regulated protein expression protease inhibitor |
| CA1329760C (fr) * | 1987-10-29 | 1994-05-24 | Ted C. K. Lee | Formulation de plasma et de proteines recombinantes dans des milieux a grande force ionique |
| WO1989009784A1 (fr) * | 1988-04-08 | 1989-10-19 | Commonwealth Serum Laboratories Commission | Production de concentre de facteur viii thermostable |
| US5780014A (en) * | 1995-04-14 | 1998-07-14 | Inhale Therapeutic Systems | Method and apparatus for pulmonary administration of dry powder alpha 1-antitrypsin |
| US6258341B1 (en) * | 1995-04-14 | 2001-07-10 | Inhale Therapeutic Systems, Inc. | Stable glassy state powder formulations |
| US5763401A (en) * | 1996-07-12 | 1998-06-09 | Bayer Corporation | Stabilized albumin-free recombinant factor VIII preparation having a low sugar content |
| DK0972520T3 (da) * | 1997-01-30 | 2005-12-19 | Bioph Biotech Entw Pharm Gmbh | Frysetörret sammensætning af humant, knoglemorfogenetisk protein MP52 |
| JP2000247903A (ja) * | 1999-03-01 | 2000-09-12 | Chugai Pharmaceut Co Ltd | 長期安定化製剤 |
| AU3556400A (en) * | 1999-03-17 | 2000-10-04 | Novartis Ag | Pharmaceutical compositions |
| EP1196187A4 (fr) * | 1999-06-02 | 2003-02-05 | Human Genome Sciences Inc | Formulations a base de fecteur de croissance keratinocytaire 2 |
| GB9930882D0 (en) * | 1999-12-30 | 2000-02-23 | Nps Allelix Corp | GLP-2 formulations |
| DE60127175T2 (de) * | 2000-12-21 | 2007-11-08 | Nektar Therapeutics, San Carlos | Lagerstabile pulverzusammensetzungen mit interleukin-4 rezeptor |
| US6887462B2 (en) * | 2001-04-09 | 2005-05-03 | Chiron Corporation | HSA-free formulations of interferon-beta |
| CN1607941A (zh) * | 2001-11-19 | 2005-04-20 | 贝克顿迪肯森公司 | 粒状药物组合物 |
| GB0207092D0 (en) * | 2002-03-26 | 2002-05-08 | Sod Conseils Rech Applic | Stable pharmaceutical composition containing factor VIII |
| US7777006B2 (en) * | 2002-12-31 | 2010-08-17 | Csl Behring L.L.C. | Method for purification of alpha-1-antitrypsin |
-
2004
- 2004-11-10 CA CA002545458A patent/CA2545458A1/fr not_active Abandoned
- 2004-11-10 EP EP04798463A patent/EP1685160A1/fr not_active Withdrawn
- 2004-11-10 JP JP2006538939A patent/JP2007534633A/ja active Pending
- 2004-11-10 AU AU2004288854A patent/AU2004288854B2/en not_active Ceased
- 2004-11-10 WO PCT/GB2004/004740 patent/WO2005047323A1/fr not_active Ceased
Also Published As
| Publication number | Publication date |
|---|---|
| WO2005047323A1 (fr) | 2005-05-26 |
| JP2007534633A (ja) | 2007-11-29 |
| EP1685160A1 (fr) | 2006-08-02 |
| AU2004288854B2 (en) | 2009-10-01 |
| AU2004288854A1 (en) | 2005-05-26 |
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Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| EEER | Examination request | ||
| FZDE | Dead |
Effective date: 20121113 |