JP5933526B2 - 免疫グロブリン結合性新規ポリペプチド - Google Patents
免疫グロブリン結合性新規ポリペプチド Download PDFInfo
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- JP5933526B2 JP5933526B2 JP2013507569A JP2013507569A JP5933526B2 JP 5933526 B2 JP5933526 B2 JP 5933526B2 JP 2013507569 A JP2013507569 A JP 2013507569A JP 2013507569 A JP2013507569 A JP 2013507569A JP 5933526 B2 JP5933526 B2 JP 5933526B2
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- ZPNFWUPYTFPOJU-LPYSRVMUSA-N iniprol Chemical compound C([C@H]1C(=O)NCC(=O)NCC(=O)N[C@H]2CSSC[C@H]3C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C(N[C@H](C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC=4C=CC=CC=4)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC=4C=CC=CC=4)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC2=O)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC=2C=CC=CC=2)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H]2N(CCC2)C(=O)[C@@H](N)CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N2[C@@H](CCC2)C(=O)N2[C@@H](CCC2)C(=O)N[C@@H](CC=2C=CC(O)=CC=2)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N2[C@@H](CCC2)C(=O)N3)C(=O)NCC(=O)NCC(=O)N[C@@H](C)C(O)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@H](C(=O)N1)C(C)C)[C@@H](C)O)[C@@H](C)CC)=O)[C@@H](C)CC)C1=CC=C(O)C=C1 ZPNFWUPYTFPOJU-LPYSRVMUSA-N 0.000 description 1
- 150000002505 iron Chemical class 0.000 description 1
- 229910000358 iron sulfate Inorganic materials 0.000 description 1
- BAUYGSIQEAFULO-UHFFFAOYSA-L iron(2+) sulfate (anhydrous) Chemical compound [Fe+2].[O-]S([O-])(=O)=O BAUYGSIQEAFULO-UHFFFAOYSA-L 0.000 description 1
- 238000003771 laboratory diagnosis Methods 0.000 description 1
- GDBQQVLCIARPGH-ULQDDVLXSA-N leupeptin Chemical compound CC(C)C[C@H](NC(C)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C=O)CCCN=C(N)N GDBQQVLCIARPGH-ULQDDVLXSA-N 0.000 description 1
- 108010052968 leupeptin Proteins 0.000 description 1
- XIXADJRWDQXREU-UHFFFAOYSA-M lithium acetate Chemical compound [Li+].CC([O-])=O XIXADJRWDQXREU-UHFFFAOYSA-M 0.000 description 1
- 238000011068 loading method Methods 0.000 description 1
- 159000000003 magnesium salts Chemical class 0.000 description 1
- 229910052943 magnesium sulfate Inorganic materials 0.000 description 1
- 235000019341 magnesium sulphate Nutrition 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
- 150000002696 manganese Chemical class 0.000 description 1
- 235000002867 manganese chloride Nutrition 0.000 description 1
- 239000011565 manganese chloride Substances 0.000 description 1
- 229940099607 manganese chloride Drugs 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 239000011259 mixed solution Substances 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000002715 modification method Methods 0.000 description 1
- ZIUHHBKFKCYYJD-UHFFFAOYSA-N n,n'-methylenebisacrylamide Chemical compound C=CC(=O)NCNC(=O)C=C ZIUHHBKFKCYYJD-UHFFFAOYSA-N 0.000 description 1
- 239000013642 negative control Substances 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 238000006386 neutralization reaction Methods 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 102000039446 nucleic acids Human genes 0.000 description 1
- 108020004707 nucleic acids Proteins 0.000 description 1
- 150000007523 nucleic acids Chemical class 0.000 description 1
- 239000002773 nucleotide Substances 0.000 description 1
- 125000003729 nucleotide group Chemical group 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- 239000003960 organic solvent Substances 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 229940049954 penicillin Drugs 0.000 description 1
- 108010091212 pepstatin Proteins 0.000 description 1
- FAXGPCHRFPCXOO-LXTPJMTPSA-N pepstatin A Chemical compound OC(=O)C[C@H](O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)C[C@H](O)[C@H](CC(C)C)NC(=O)[C@H](C(C)C)NC(=O)[C@H](C(C)C)NC(=O)CC(C)C FAXGPCHRFPCXOO-LXTPJMTPSA-N 0.000 description 1
- 239000000137 peptide hydrolase inhibitor Substances 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 229920000058 polyacrylate Polymers 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 238000003752 polymerase chain reaction Methods 0.000 description 1
- 210000004896 polypeptide structure Anatomy 0.000 description 1
- 229920001282 polysaccharide Polymers 0.000 description 1
- 239000005017 polysaccharide Substances 0.000 description 1
- 229920002223 polystyrene Polymers 0.000 description 1
- 229920002451 polyvinyl alcohol Polymers 0.000 description 1
- XAEFZNCEHLXOMS-UHFFFAOYSA-M potassium benzoate Chemical compound [K+].[O-]C(=O)C1=CC=CC=C1 XAEFZNCEHLXOMS-UHFFFAOYSA-M 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 210000001236 prokaryotic cell Anatomy 0.000 description 1
- 238000001742 protein purification Methods 0.000 description 1
- 239000012460 protein solution Substances 0.000 description 1
- 239000012521 purified sample Substances 0.000 description 1
- 238000010223 real-time analysis Methods 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 102220002405 rs121908660 Human genes 0.000 description 1
- 239000012146 running buffer Substances 0.000 description 1
- 239000013605 shuttle vector Substances 0.000 description 1
- 239000000741 silica gel Substances 0.000 description 1
- 229910002027 silica gel Inorganic materials 0.000 description 1
- 239000001632 sodium acetate Substances 0.000 description 1
- 235000017281 sodium acetate Nutrition 0.000 description 1
- 159000000000 sodium salts Chemical class 0.000 description 1
- 230000003381 solubilizing effect Effects 0.000 description 1
- 125000006850 spacer group Chemical group 0.000 description 1
- 238000010186 staining Methods 0.000 description 1
- 230000001954 sterilising effect Effects 0.000 description 1
- 238000004659 sterilization and disinfection Methods 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 239000005720 sucrose Substances 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 239000004094 surface-active agent Substances 0.000 description 1
- 229920001059 synthetic polymer Polymers 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 238000013519 translation Methods 0.000 description 1
- 238000001262 western blot Methods 0.000 description 1
- 150000003751 zinc Chemical class 0.000 description 1
- 235000005074 zinc chloride Nutrition 0.000 description 1
- 239000011592 zinc chloride Substances 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
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/305—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Micrococcaceae (F)
- C07K14/31—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Micrococcaceae (F) from Staphylococcus (G)
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
-
- 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
Description
RFX1X2EQQNAFYEILHX3PNLTEEQRNX4FIQX5LX6X7X8PSVSREX9LAEAX10X11LNDAQAPX12
(前記アミノ酸配列中、
X1 = D, E, N,又は Q
X2 = E,又は R
X3 = L, M,又は I
X4 = A, E, F, R, Y,又は W
X5 = D, E, H, I, L, Q, R, S, T,又は V
X6 = H, I,又は R
X7 = D, I,又は R
X8 = D,又は E
X9 = I, L,又は V
X10 = R,又は Q
X11 = H,又は R
X12 = R, G,又は K
である)
を含み、免疫グロブリンのFc領域を含むタンパク質に結合することを特徴とするポリペプチドに関する。
Z1Z2Z3RFX1X2EQQNAFYEILHX3PNLTEEQRNX4FIQX5LX6X7X8PSVSREX9LAEAX10X11LNDAQAPX12
(前記アミノ酸配列中、
X1 = D, E, N,又は Q
X2 = E,又は R
X3 = L, M,又は I
X4 = A, E, F, R, Y,又は W
X5 = D, E, H, I, L, Q, R, S, T,又は V
X6 = H, I,又は R
X7 = D, I,又は R
X8 = D,又は E
X9 = I, L,又は V
X10 = R,又は Q
X11 = H,又は R
X12 = R, G,又は K
Z1〜Z3 = A, D, E, G, H, I, L, N, Q, R, S, T, V,又は Y
である)
を含み、免疫グロブリンのFc領域を含むタンパク質に結合することを特徴とするポリペプチドに関する。
ADNRFNREQQNAFYEILHLPNLTEEQRNAFIQSLRDDPSVSREILAEARRLNDAQAPG(配列番号1)、又は
ADNRFNREQQNAFYEILHLPNLTEEQRNAFIQSLRDDPSVSREILAEARRLNDAQAPR(配列番号2)
との配列同一性が90%以上であることが好ましい。
RFX1X2EQQNAFYEILHX3PNLTEEQRNX4FIQX5LX6X7X8PSVSREX9LAEAX10X11LNDAQAPX12
X1 = D, E, N,又は Q
X2 = E,又は R
X3 = L, M,又は I
X4 = A, E, F, R, Y,又は W
X5 = D, E, H, I, L, Q, R, S, T,又は V
X6 = H, I,又は R
X7 = D, I,又は R
X8 = D,又は E
X9 = I, L,又は V
X10 = R,又は Q
X11 = H,又は R
X12 = R, G,又は K
Z1Z2Z3RFX1X2EQQNAFYEILHX3PNLTEEQRNX4FIQX5LX6X7X8PSVSREX9LAEAX10X11LNDAQAPX12
X1 = D, E, N,又は Q
X2 = E,又は R
X3 = L, M,又は I
X4 = A, E, F, R, Y,又は W
X5 = D, E, H, I, L, Q, R, S, T,又は V
X6 = H, I,又は R
X7 = D, I,又は R
X8 = D,又は E
X9 = I, L,又は V
X10 = R,又は Q
X11 = H,又は R
X12 = R, G,又は K
Z1〜Z3 = A, D, E, G, H, I, L, N, Q, R, S, T, V, 又は Y
ADNRFNREQQNAFYEILHLPNLTEEQRNAFIQSLRDDPSVSREILAEARRLNDAQAPG(配列番号1)、又は
ADNRFNREQQNAFYEILHLPNLTEEQRNAFIQSLRDDPSVSREILAEARRLNDAQAPR(配列番号2)
配列番号3および4に記載のヌクレオチド配列を有するオリゴヌクレオチドを混合し、ポリメラーゼにBlend Taq(東洋紡績株式会社製)を用い、添付のプロトコルに従ってオーバーラップPCR反応を行った。PCR反応生成物である二本鎖DNAをアガロース電気泳動で抽出・精製し、制限酵素BamHIとHindIII(いずれもタカラバイオ株式会社製)により切断した。同様の手法で、配列番号5および6に記載のヌクレオチド配列を有するオリゴヌクレオチドから、PCR反応にて目的の二本鎖DNAを得て、制限酵素HindIIIとEcoRI(タカラバイオ株式会社製)により切断した。
表面プラズモン共鳴を利用したバイオセンサーBiacore 3000(GEヘルスケア・ジャパン株式会社製)を用いて、実施例1で取得した各種ポリペプチドの免疫グロブリンとの親和性を解析した。
実施例1で取得した各種ポリペプチドについて、アルカリ性条件下で一定時間インキュベートする処理を行った後の、SDS−PAGE上のバンドの状態を比較することで評価した。
実施例1で取得した配列番号1をコードするDNAを含むpGEX−2Tを鋳型DNAとして、2種類のプライマーを用いて、クイックチェンジ法を実施し、新たな変異を含む発現プラスミドを取得した。クイックチェンジ法は、DNAポリメラーゼのPfu Turbo、および、メチル化DNA(鋳型DNA)切断酵素DpnI(ともにStratagene社製)を用い、Stratagene社のプロトコルに従い実施した。配列番号16と17、または、配列番号18と19、または、配列番号20と21、または、配列番号22と23、配列番号24と25、配列番号26と27、配列番号28と29という、7通りのプライマーの組み合わせで、新たな変異を導入した発現プラスミドを調製した。さらに、配列番号16と17のプライマーを用いて調製した発現プラスミドを鋳型DNAとして、配列番号18と19のプライマーを用いて、もう一度変異を導入した発現プラスミドも調製した。したがって、新たに8種類の発現プラスミドを調製した。
ADNRFNREQQNAFYEILHLPNLTEEQRNAFIQSLRDDPSVSREILAEAQRLNDAQAPR(配列番号30)
ADNRFNREQQNAFYEILHLPNLTEEQRNAFIQSLIDDPSVSREILAEAQRLNDAQAPR(配列番号31)
ADNRFNREQQNAFYEILHLPNLTEEQRNAFIQSLIDDPSVSREILAEARRLNDAQAPR(配列番号32)
ADNRFNREQQNAFYEILHLPNLTEEQRNAFIQSLHDDPSVSREILAEARRLNDAQAPR(配列番号33)
ADNRFNREQQNAFYEILHLPNLTEEQRNAFIQELRDDPSVSREILAEARRLNDAQAPR(配列番号34)
ADNRFNREQQNAFYEILHLPNLTEEQRNAFIQLLRDDPSVSREILAEARRLNDAQAPR(配列番号35)
ADNRFNREQQNAFYEILHLPNLTEEQRNAFIQTLRDDPSVSREILAEARRLNDAQAPR(配列番号36)
ADNRFNREQQNAFYEILHLPNLTEEQRNAFIQSLRIDPSVSREILAEARRLNDAQAPR(配列番号37)
実施例4で取得した各種ポリペプチドについて、実施例3と同様の手法にて、アルカリ性条件下で一定時間インキュベートする処理を行った後の、SDS−PAGE上のバンドの状態を比較することで評価した。配列番号38〜41のポリペプチドについては、4時間及び24時間インキュベートした後の安定性を評価した。配列番号42〜45のポリペプチドについては、30時間インキュベートした後の安定性を評価した。なお、参照として配列番号14のポリペプチドについても同様の操作を行った。
C−G29A.2dはプロテインAのCドメインに変異G29Aを導入した等機能変異体であり、アルカリ耐性が非常に高いことで公知(特許文献5)のポリペプチドである。この等機能変異体がタンデムに連結されたポリペプチド(配列番号15)をコードするDNAを、PstI/EcoRIサイトで切断できるようにPCRで増幅し、ベクターpNK3260’にサブクローニングした。実施例1と同様の方法で発現・精製を行い、実施例3と同様の方法でアルカリ耐性を評価した。
C−G29Aに変異S33Eを導入したポリペプチドは、C−G29Aと同等のアルカリ耐性を示す公知のポリペプチドである(国際公開第2011/118699号公報)。この配列がタンデムに連結されたポリペプチド(配列番号46)について、実施例1と同様の手法で発現・精製を行い、実施例3と同様の方法でアルカリ耐性を評価した。
Claims (3)
- 以下のアミノ酸配列:
RFX1X2EQQNAFYEILHX3PNLTEEQRNX4FIQX5LX6X7X8PSVSREX9LAEAX10X11LNDAQAPX12
(前記アミノ酸配列中、
X1 = N
X2 = R
X3 = L
X4 = A
X5 = E,L,S,又はT
X6 = H,I,又はR
X7 = D,又はI
X8 = D
X9 = I
X10 = R,又はQ
X11 = R
X12 = R,又はG
である)
を含み、免疫グロブリンのFc領域を含むタンパク質に結合することを特徴とするポリペプチド。 - 以下のアミノ酸配列:
Z1Z2Z3RFX1X2EQQNAFYEILHX3PNLTEEQRNX4FIQX5LX6X7X8PSVSREX9LAEAX10X11LNDAQAPX12
(前記アミノ酸配列中、
X1 = N
X2 = R
X3 = L
X4 = A
X5 = E,L,S,又はT
X6 = H,I,又はR
X7 = D,又はI
X8 = D
X9 = I
X10 = R,又はQ
X11 = R
X12 = R,又はG
Z1〜Z3 = A,D,E,G,H,I,L,N,Q,R,S,T,V,又はY
である)
を含み、免疫グロブリンのFc領域を含むタンパク質に結合することを特徴とするポリペプチド。 - 以下のアミノ酸配列:
ADNRFNREQQNAFYEILHLPNLTEEQRNAFIQSLRDDPSVSREILAEARRLNDAQAPG(配列番号1)、又は
ADNRFNREQQNAFYEILHLPNLTEEQRNAFIQSLRDDPSVSREILAEARRLNDAQAPR(配列番号2)
との配列同一性が90%以上である、請求項1又は2に記載のポリペプチド。
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JP2011068497 | 2011-03-25 | ||
PCT/JP2012/057799 WO2012133342A1 (ja) | 2011-03-25 | 2012-03-26 | 免疫グロブリン結合性新規ポリペプチド |
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JPWO2012133342A1 JPWO2012133342A1 (ja) | 2014-07-28 |
JP5933526B2 true JP5933526B2 (ja) | 2016-06-08 |
Family
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US (1) | US9284354B2 (ja) |
EP (1) | EP2690108B1 (ja) |
JP (1) | JP5933526B2 (ja) |
KR (1) | KR20140007394A (ja) |
CN (1) | CN103443120B (ja) |
AU (1) | AU2012233980B2 (ja) |
CA (1) | CA2830990A1 (ja) |
SG (1) | SG193950A1 (ja) |
WO (1) | WO2012133342A1 (ja) |
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WO2012133349A1 (ja) | 2011-03-25 | 2012-10-04 | 株式会社カネカ | アフィニティー分離マトリックス用タンパク質 |
WO2014046278A1 (ja) * | 2012-09-21 | 2014-03-27 | 株式会社カネカ | アフィニティー分離マトリックス用タンパク質リガンド |
US20160215026A1 (en) * | 2013-09-06 | 2016-07-28 | Kaneka Corporation | Dissociation capacity-boosted ligand for affinity dissociation matrix |
CN104945488B (zh) * | 2014-03-27 | 2020-02-18 | 迈格生物医药(上海)有限公司 | 一种具有免疫球蛋白结合能力的多肽 |
KR101964619B1 (ko) * | 2014-09-29 | 2019-04-02 | 후지필름 가부시키가이샤 | 항체 결합성 폴리펩타이드, 항체 결합성 융합 폴리펩타이드 및 흡착 재료 |
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KR20140007394A (ko) | 2014-01-17 |
EP2690108A1 (en) | 2014-01-29 |
US20140100356A1 (en) | 2014-04-10 |
SG193950A1 (en) | 2013-11-29 |
EP2690108A4 (en) | 2014-12-31 |
JPWO2012133342A1 (ja) | 2014-07-28 |
CN103443120B (zh) | 2016-08-31 |
AU2012233980B2 (en) | 2016-10-13 |
CN103443120A (zh) | 2013-12-11 |
US9284354B2 (en) | 2016-03-15 |
AU2012233980A1 (en) | 2013-10-17 |
EP2690108B1 (en) | 2018-07-25 |
CA2830990A1 (en) | 2012-10-04 |
WO2012133342A1 (ja) | 2012-10-04 |
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