CA2793144A1 - Use of achromopeptidase for lysis at room temperature - Google Patents
Use of achromopeptidase for lysis at room temperature Download PDFInfo
- Publication number
- CA2793144A1 CA2793144A1 CA2793144A CA2793144A CA2793144A1 CA 2793144 A1 CA2793144 A1 CA 2793144A1 CA 2793144 A CA2793144 A CA 2793144A CA 2793144 A CA2793144 A CA 2793144A CA 2793144 A1 CA2793144 A1 CA 2793144A1
- Authority
- CA
- Canada
- Prior art keywords
- biological sample
- sample
- achromopeptidase
- nucleic acids
- target
- 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
- 108010053229 Lysyl endopeptidase Proteins 0.000 title claims abstract description 48
- 230000009089 cytolysis Effects 0.000 title description 44
- 239000000523 sample Substances 0.000 claims abstract description 71
- 238000000034 method Methods 0.000 claims abstract description 51
- 108020004707 nucleic acids Proteins 0.000 claims abstract description 51
- 150000007523 nucleic acids Chemical class 0.000 claims abstract description 51
- 102000039446 nucleic acids Human genes 0.000 claims abstract description 51
- 239000012472 biological sample Substances 0.000 claims abstract description 37
- 241000894006 Bacteria Species 0.000 claims abstract description 24
- UQSXHKLRYXJYBZ-UHFFFAOYSA-N iron oxide Inorganic materials [Fe]=O UQSXHKLRYXJYBZ-UHFFFAOYSA-N 0.000 claims abstract description 23
- 230000001413 cellular effect Effects 0.000 claims abstract description 16
- NDLPOXTZKUMGOV-UHFFFAOYSA-N oxo(oxoferriooxy)iron hydrate Chemical compound O.O=[Fe]O[Fe]=O NDLPOXTZKUMGOV-UHFFFAOYSA-N 0.000 claims abstract description 16
- 241000192125 Firmicutes Species 0.000 claims abstract description 15
- 230000002934 lysing effect Effects 0.000 claims abstract description 14
- 241000191967 Staphylococcus aureus Species 0.000 claims abstract description 10
- 241000193985 Streptococcus agalactiae Species 0.000 claims abstract description 8
- 239000000243 solution Substances 0.000 claims description 22
- 239000002245 particle Substances 0.000 claims description 16
- 239000002953 phosphate buffered saline Substances 0.000 claims description 13
- 239000000872 buffer Substances 0.000 claims description 11
- 241001153886 Ami Species 0.000 claims description 8
- 230000035899 viability Effects 0.000 claims description 6
- 238000003556 assay Methods 0.000 claims description 5
- 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 claims description 5
- VLEIUWBSEKKKFX-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;2-[2-[bis(carboxymethyl)amino]ethyl-(carboxymethyl)amino]acetic acid Chemical compound OCC(N)(CO)CO.OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O VLEIUWBSEKKKFX-UHFFFAOYSA-N 0.000 claims description 4
- RJQXTJLFIWVMTO-TYNCELHUSA-N Methicillin Chemical compound COC1=CC=CC(OC)=C1C(=O)N[C@@H]1C(=O)N2[C@@H](C(O)=O)C(C)(C)S[C@@H]21 RJQXTJLFIWVMTO-TYNCELHUSA-N 0.000 claims description 4
- 239000008280 blood Substances 0.000 claims description 4
- 210000004369 blood Anatomy 0.000 claims description 4
- 229960003085 meticillin Drugs 0.000 claims description 4
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 4
- 150000003839 salts Chemical class 0.000 claims description 3
- 239000002689 soil Substances 0.000 claims description 3
- 210000002700 urine Anatomy 0.000 claims description 3
- 206010036790 Productive cough Diseases 0.000 claims description 2
- 210000003608 fece Anatomy 0.000 claims description 2
- 210000003097 mucus Anatomy 0.000 claims description 2
- 210000003296 saliva Anatomy 0.000 claims description 2
- 210000000582 semen Anatomy 0.000 claims description 2
- 210000003802 sputum Anatomy 0.000 claims description 2
- 208000024794 sputum Diseases 0.000 claims description 2
- 244000005700 microbiome Species 0.000 claims 9
- 239000003795 chemical substances by application Substances 0.000 abstract description 6
- 238000003752 polymerase chain reaction Methods 0.000 abstract description 5
- 230000002255 enzymatic effect Effects 0.000 abstract description 4
- 241000124008 Mammalia Species 0.000 abstract description 2
- 230000008569 process Effects 0.000 abstract description 2
- 238000000605 extraction Methods 0.000 description 40
- 108020004414 DNA Proteins 0.000 description 22
- 230000001580 bacterial effect Effects 0.000 description 19
- 238000001514 detection method Methods 0.000 description 13
- 239000002609 medium Substances 0.000 description 13
- 101100468275 Caenorhabditis elegans rep-1 gene Proteins 0.000 description 11
- 238000011534 incubation Methods 0.000 description 9
- 239000006163 transport media Substances 0.000 description 9
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 8
- 238000004458 analytical method Methods 0.000 description 7
- 239000000470 constituent Substances 0.000 description 7
- 210000002421 cell wall Anatomy 0.000 description 6
- 238000006243 chemical reaction Methods 0.000 description 6
- 238000003745 diagnosis Methods 0.000 description 6
- 230000000694 effects Effects 0.000 description 6
- 230000001420 bacteriolytic effect Effects 0.000 description 5
- 210000004027 cell Anatomy 0.000 description 5
- 230000002101 lytic effect Effects 0.000 description 5
- 238000007789 sealing Methods 0.000 description 5
- 239000011780 sodium chloride Substances 0.000 description 5
- 108090000790 Enzymes Proteins 0.000 description 4
- 102000004190 Enzymes Human genes 0.000 description 4
- 108091092584 GDNA Proteins 0.000 description 4
- 241000271897 Viperidae Species 0.000 description 4
- 229940088598 enzyme Drugs 0.000 description 4
- 235000010335 lysozyme Nutrition 0.000 description 4
- 241000894007 species Species 0.000 description 4
- 238000012360 testing method Methods 0.000 description 4
- 108010014251 Muramidase Proteins 0.000 description 3
- 102000016943 Muramidase Human genes 0.000 description 3
- MSFSPUZXLOGKHJ-UHFFFAOYSA-N Muraminsaeure Natural products OC(=O)C(C)OC1C(N)C(O)OC(CO)C1O MSFSPUZXLOGKHJ-UHFFFAOYSA-N 0.000 description 3
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 3
- 108010013639 Peptidoglycan Proteins 0.000 description 3
- 108010006785 Taq Polymerase Proteins 0.000 description 3
- 238000007796 conventional method Methods 0.000 description 3
- 229960000274 lysozyme Drugs 0.000 description 3
- 239000004325 lysozyme Substances 0.000 description 3
- 230000007246 mechanism Effects 0.000 description 3
- 239000012528 membrane Substances 0.000 description 3
- 230000002797 proteolythic effect Effects 0.000 description 3
- 108020000946 Bacterial DNA Proteins 0.000 description 2
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 2
- 238000007400 DNA extraction Methods 0.000 description 2
- TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 2
- WCUXLLCKKVVCTQ-UHFFFAOYSA-M Potassium chloride Chemical compound [Cl-].[K+] WCUXLLCKKVVCTQ-UHFFFAOYSA-M 0.000 description 2
- 230000002411 adverse Effects 0.000 description 2
- 230000008901 benefit Effects 0.000 description 2
- 210000001124 body fluid Anatomy 0.000 description 2
- 239000010839 body fluid Substances 0.000 description 2
- 239000001110 calcium chloride Substances 0.000 description 2
- 229910001628 calcium chloride Inorganic materials 0.000 description 2
- 239000003153 chemical reaction reagent Substances 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- -1 genomic DNA Chemical class 0.000 description 2
- 208000015181 infectious disease Diseases 0.000 description 2
- 238000002955 isolation Methods 0.000 description 2
- 235000019796 monopotassium phosphate Nutrition 0.000 description 2
- 244000052769 pathogen Species 0.000 description 2
- GNSKLFRGEWLPPA-UHFFFAOYSA-M potassium dihydrogen phosphate Chemical compound [K+].OP(O)([O-])=O GNSKLFRGEWLPPA-UHFFFAOYSA-M 0.000 description 2
- 238000011084 recovery Methods 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 241000606153 Chlamydia trachomatis Species 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
- 101000925662 Enterobacteria phage PRD1 Endolysin Proteins 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 241000588652 Neisseria gonorrhoeae Species 0.000 description 1
- 239000007984 Tris EDTA buffer Substances 0.000 description 1
- 239000007983 Tris buffer Substances 0.000 description 1
- 230000003321 amplification Effects 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 244000052616 bacterial pathogen Species 0.000 description 1
- 230000006037 cell lysis Effects 0.000 description 1
- 210000000170 cell membrane Anatomy 0.000 description 1
- 230000003833 cell viability Effects 0.000 description 1
- 229940038705 chlamydia trachomatis Drugs 0.000 description 1
- 238000011109 contamination Methods 0.000 description 1
- 238000004132 cross linking Methods 0.000 description 1
- 239000005547 deoxyribonucleotide Substances 0.000 description 1
- 125000002637 deoxyribonucleotide group Chemical group 0.000 description 1
- 238000002405 diagnostic procedure Methods 0.000 description 1
- 229940111685 dibasic potassium phosphate Drugs 0.000 description 1
- 238000007865 diluting Methods 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- ZPWVASYFFYYZEW-UHFFFAOYSA-L dipotassium hydrogen phosphate Chemical compound [K+].[K+].OP([O-])([O-])=O ZPWVASYFFYYZEW-UHFFFAOYSA-L 0.000 description 1
- BNIILDVGGAEEIG-UHFFFAOYSA-L disodium hydrogen phosphate Chemical compound [Na+].[Na+].OP([O-])([O-])=O BNIILDVGGAEEIG-UHFFFAOYSA-L 0.000 description 1
- 229910000397 disodium phosphate Inorganic materials 0.000 description 1
- 235000019800 disodium phosphate Nutrition 0.000 description 1
- 238000011143 downstream manufacturing Methods 0.000 description 1
- 239000003480 eluent Substances 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 239000012530 fluid Substances 0.000 description 1
- 239000012634 fragment Substances 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- 150000004676 glycans Chemical group 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 238000011835 investigation Methods 0.000 description 1
- 229910001629 magnesium chloride Inorganic materials 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 229940111688 monobasic potassium phosphate Drugs 0.000 description 1
- 229910000402 monopotassium phosphate Inorganic materials 0.000 description 1
- 238000003199 nucleic acid amplification method Methods 0.000 description 1
- 239000002773 nucleotide Substances 0.000 description 1
- 125000003729 nucleotide group Chemical group 0.000 description 1
- 239000001103 potassium chloride Substances 0.000 description 1
- 235000011164 potassium chloride Nutrition 0.000 description 1
- LWIHDJKSTIGBAC-UHFFFAOYSA-K potassium phosphate Substances [K+].[K+].[K+].[O-]P([O-])([O-])=O LWIHDJKSTIGBAC-UHFFFAOYSA-K 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 229960002901 sodium glycerophosphate Drugs 0.000 description 1
- 239000001488 sodium phosphate Substances 0.000 description 1
- GNBVPFITFYNRCN-UHFFFAOYSA-M sodium thioglycolate Chemical compound [Na+].[O-]C(=O)CS GNBVPFITFYNRCN-UHFFFAOYSA-M 0.000 description 1
- 229940046307 sodium thioglycolate Drugs 0.000 description 1
- REULQIKBNNDNDX-UHFFFAOYSA-M sodium;2,3-dihydroxypropyl hydrogen phosphate Chemical compound [Na+].OCC(O)COP(O)([O-])=O REULQIKBNNDNDX-UHFFFAOYSA-M 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 230000008685 targeting Effects 0.000 description 1
- 238000004448 titration Methods 0.000 description 1
- 239000001226 triphosphate Substances 0.000 description 1
- 235000011178 triphosphate Nutrition 0.000 description 1
- UNXRWKVEANCORM-UHFFFAOYSA-N triphosphoric acid Chemical compound OP(O)(=O)OP(O)(=O)OP(O)(O)=O UNXRWKVEANCORM-UHFFFAOYSA-N 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/10—Processes for the isolation, preparation or purification of DNA or RNA
- C12N15/1003—Extracting or separating nucleic acids from biological samples, e.g. pure separation or isolation methods; Conditions, buffers or apparatuses therefor
- C12N15/1006—Extracting or separating nucleic acids from biological samples, e.g. pure separation or isolation methods; Conditions, buffers or apparatuses therefor by means of a solid support carrier, e.g. particles, polymers
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/10—Processes for the isolation, preparation or purification of DNA or RNA
- C12N15/1003—Extracting or separating nucleic acids from biological samples, e.g. pure separation or isolation methods; Conditions, buffers or apparatuses therefor
- C12N15/1006—Extracting or separating nucleic acids from biological samples, e.g. pure separation or isolation methods; Conditions, buffers or apparatuses therefor by means of a solid support carrier, e.g. particles, polymers
- C12N15/1013—Extracting or separating nucleic acids from biological samples, e.g. pure separation or isolation methods; Conditions, buffers or apparatuses therefor by means of a solid support carrier, e.g. particles, polymers by using magnetic beads
Landscapes
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Health & Medical Sciences (AREA)
- Biomedical Technology (AREA)
- Life Sciences & Earth Sciences (AREA)
- Genetics & Genomics (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Organic Chemistry (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Biotechnology (AREA)
- General Engineering & Computer Science (AREA)
- Crystallography & Structural Chemistry (AREA)
- Plant Pathology (AREA)
- Molecular Biology (AREA)
- Microbiology (AREA)
- Biophysics (AREA)
- Physics & Mathematics (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Analytical Chemistry (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US31431810P | 2010-03-16 | 2010-03-16 | |
| US61/314,318 | 2010-03-16 | ||
| PCT/US2011/028494 WO2011115975A2 (en) | 2010-03-16 | 2011-03-15 | Use of achromopeptidase for lysis at room temperature |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA2793144A1 true CA2793144A1 (en) | 2011-09-22 |
Family
ID=44649786
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA2793144A Abandoned CA2793144A1 (en) | 2010-03-16 | 2011-03-15 | Use of achromopeptidase for lysis at room temperature |
Country Status (8)
| Country | Link |
|---|---|
| US (1) | US20110275090A1 (enExample) |
| EP (1) | EP2547767A4 (enExample) |
| JP (1) | JP2013521804A (enExample) |
| CN (1) | CN102869773A (enExample) |
| AU (1) | AU2011227452B2 (enExample) |
| BR (1) | BR112012023875A2 (enExample) |
| CA (1) | CA2793144A1 (enExample) |
| WO (1) | WO2011115975A2 (enExample) |
Families Citing this family (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US8597884B2 (en) | 2011-03-09 | 2013-12-03 | Becton, Dickinson And Company | Process controls for molecular assay |
| US9528987B2 (en) | 2011-06-23 | 2016-12-27 | University Of Washington | Reagent patterning in capillarity-based analyzers and associated systems and methods |
| WO2013117968A1 (en) | 2012-02-10 | 2013-08-15 | Reametrix Inc. | Methods for lysing bacteria from sample and isolating cellular components therefrom, and kits therefor |
| EP2948249A1 (en) | 2013-01-22 | 2015-12-02 | University of Washington through its Center for Commercialization | Sequential delivery of fluid volumes and associated devices, systems and methods |
| EP3320966B1 (en) | 2016-11-14 | 2022-02-16 | Airbus Operations GmbH | Autoclave and method for welding thermoplastic composite parts |
| CN111278844B (zh) * | 2017-09-13 | 2023-12-19 | 贝克顿·迪金森公司 | 用于使用氧化铁颗粒提取核酸的方法和组合物 |
| WO2021217173A1 (en) * | 2020-04-21 | 2021-10-28 | Siemens Healthcare Diagnostics Inc. | Clinical specimen collection swabs for molecular diagnostic applications and methods of production and use thereof |
| CN118834934B (zh) * | 2024-08-19 | 2025-05-16 | 希莱乐检(郑州)生物科技有限公司 | 用于结核分枝杆菌核酸释放的裂解液及其应用 |
Family Cites Families (15)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB8414273D0 (en) * | 1984-06-05 | 1984-07-11 | Oxoid Ltd | Identifying streptococcal grouping |
| JP2589729B2 (ja) * | 1988-01-30 | 1997-03-12 | 極東製薬工業株式会社 | 染色体ｄｎａを用いた細菌の同定方法および該同定用キット |
| JPH06510363A (ja) * | 1990-10-29 | 1994-11-17 | ディカルブ プラント ジェネティクス | 磁気性粒子を使用する生物学的材料の単離 |
| US5185242A (en) * | 1991-06-24 | 1993-02-09 | Becton Dickinson And Company | Method for lysing mycobacteria using achromopeptidase |
| US5973138A (en) * | 1998-10-30 | 1999-10-26 | Becton Dickinson And Company | Method for purification and manipulation of nucleic acids using paramagnetic particles |
| JP3172917B2 (ja) * | 1999-07-23 | 2001-06-04 | 北海道 | 細菌検出方法 |
| US20040002594A1 (en) * | 2002-06-27 | 2004-01-01 | John Krupey | Removal of extraneous substances from biological fluids containing nucleic acids and the recovery of nucleic acids |
| US7595176B2 (en) * | 2003-05-30 | 2009-09-29 | Georgia Tech Research Corporation | Methods and reagents for quantitative analysis of Dehalococcoides species |
| WO2005064016A1 (ja) * | 2003-12-26 | 2005-07-14 | Prima Meat Packers, Ltd. | 微生物の多重検出方法 |
| US20060057613A1 (en) * | 2004-07-26 | 2006-03-16 | Nanosphere, Inc. | Method for distinguishing methicillin resistant S. aureus from methicillin sensitive S. aureus in a mixed culture |
| AU2006271104B2 (en) * | 2005-07-21 | 2011-01-27 | Morinaga Milk Industry Co., Ltd. | Method for detection of microorganism and kit for detection of microorganism |
| JP2010510524A (ja) * | 2006-11-22 | 2010-04-02 | スリーエム イノベイティブ プロパティズ カンパニー | 試料を調製及び分析するシステム並びに方法 |
| JP2008148570A (ja) * | 2006-12-14 | 2008-07-03 | Hitachi Ltd | 微生物検出システム |
| US20090215050A1 (en) * | 2008-02-22 | 2009-08-27 | Robert Delmar Jenison | Systems and methods for point-of-care amplification and detection of polynucleotides |
| US20090274577A1 (en) * | 2008-05-05 | 2009-11-05 | B-K Medical Aps | Sterilization by treatment with reductant and oxidant |
-
2011
- 2011-03-15 WO PCT/US2011/028494 patent/WO2011115975A2/en not_active Ceased
- 2011-03-15 JP JP2013500151A patent/JP2013521804A/ja active Pending
- 2011-03-15 CN CN2011800203890A patent/CN102869773A/zh active Pending
- 2011-03-15 US US13/048,539 patent/US20110275090A1/en not_active Abandoned
- 2011-03-15 EP EP11756845.1A patent/EP2547767A4/en not_active Withdrawn
- 2011-03-15 CA CA2793144A patent/CA2793144A1/en not_active Abandoned
- 2011-03-15 BR BR112012023875A patent/BR112012023875A2/pt not_active Application Discontinuation
- 2011-03-15 AU AU2011227452A patent/AU2011227452B2/en not_active Ceased
Also Published As
| Publication number | Publication date |
|---|---|
| JP2013521804A (ja) | 2013-06-13 |
| US20110275090A1 (en) | 2011-11-10 |
| AU2011227452A1 (en) | 2012-10-04 |
| WO2011115975A3 (en) | 2012-01-19 |
| WO2011115975A2 (en) | 2011-09-22 |
| CN102869773A (zh) | 2013-01-09 |
| EP2547767A4 (en) | 2013-12-25 |
| AU2011227452B2 (en) | 2015-04-09 |
| BR112012023875A2 (pt) | 2015-09-22 |
| EP2547767A2 (en) | 2013-01-23 |
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Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| EEER | Examination request | ||
| FZDE | Discontinued |
Effective date: 20180515 |