JP2001524836A - 修飾されたアルギニンデイミナーゼ - Google Patents
修飾されたアルギニンデイミナーゼInfo
- Publication number
- JP2001524836A JP2001524836A JP54937598A JP54937598A JP2001524836A JP 2001524836 A JP2001524836 A JP 2001524836A JP 54937598 A JP54937598 A JP 54937598A JP 54937598 A JP54937598 A JP 54937598A JP 2001524836 A JP2001524836 A JP 2001524836A
- Authority
- JP
- Japan
- Prior art keywords
- group
- adi
- compound
- peg
- arginine
- 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.)
- Granted
Links
- 108010082340 Arginine deiminase Proteins 0.000 title claims abstract description 89
- 125000000637 arginyl group Chemical class N[C@@H](CCCNC(N)=N)C(=O)* 0.000 title claims 3
- 229920001223 polyethylene glycol Polymers 0.000 claims abstract description 107
- 239000002202 Polyethylene glycol Substances 0.000 claims abstract description 83
- 206010028980 Neoplasm Diseases 0.000 claims abstract description 35
- 238000000034 method Methods 0.000 claims abstract description 32
- 206010027476 Metastases Diseases 0.000 claims abstract description 11
- 230000009401 metastasis Effects 0.000 claims abstract description 6
- 239000004475 Arginine Substances 0.000 claims description 39
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 claims description 38
- 125000005647 linker group Chemical group 0.000 claims description 35
- 201000001441 melanoma Diseases 0.000 claims description 27
- 150000001875 compounds Chemical class 0.000 claims description 21
- 208000014018 liver neoplasm Diseases 0.000 claims description 17
- 201000007270 liver cancer Diseases 0.000 claims description 16
- 241000204031 Mycoplasma Species 0.000 claims description 14
- -1 succinimidyl Chemical group 0.000 claims description 13
- AASBXERNXVFUEJ-UHFFFAOYSA-N (2,5-dioxopyrrolidin-1-yl) propanoate Chemical compound CCC(=O)ON1C(=O)CCC1=O AASBXERNXVFUEJ-UHFFFAOYSA-N 0.000 claims description 11
- 125000005439 maleimidyl group Chemical group C1(C=CC(N1*)=O)=O 0.000 claims description 11
- LYCAIKOWRPUZTN-UHFFFAOYSA-N Ethylene glycol Chemical compound OCCO LYCAIKOWRPUZTN-UHFFFAOYSA-N 0.000 claims description 10
- 241000204028 Mycoplasma arginini Species 0.000 claims description 10
- QXZGLTYKKZKGLN-UHFFFAOYSA-N 4-(2,5-dioxopyrrolidin-1-yl)oxy-4-oxobutanoic acid Chemical compound OC(=O)CCC(=O)ON1C(=O)CCC1=O QXZGLTYKKZKGLN-UHFFFAOYSA-N 0.000 claims description 6
- NQTADLQHYWFPDB-UHFFFAOYSA-N N-Hydroxysuccinimide Chemical compound ON1C(=O)CCC1=O NQTADLQHYWFPDB-UHFFFAOYSA-N 0.000 claims description 6
- WGCNASOHLSPBMP-UHFFFAOYSA-N hydroxyacetaldehyde Natural products OCC=O WGCNASOHLSPBMP-UHFFFAOYSA-N 0.000 claims description 5
- 244000005700 microbiome Species 0.000 claims description 5
- 108010058207 Anistreplase Proteins 0.000 claims description 4
- 206010039491 Sarcoma Diseases 0.000 claims description 4
- 125000004185 ester group Chemical group 0.000 claims description 4
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 claims description 3
- 125000003700 epoxy group Chemical group 0.000 claims description 3
- 125000002887 hydroxy group Chemical group [H]O* 0.000 claims description 3
- 230000002401 inhibitory effect Effects 0.000 claims description 3
- KXDHJXZQYSOELW-UHFFFAOYSA-N Carbamic acid Chemical group NC(O)=O KXDHJXZQYSOELW-UHFFFAOYSA-N 0.000 claims description 2
- 150000001408 amides Chemical class 0.000 claims description 2
- 150000001720 carbohydrates Chemical group 0.000 claims description 2
- 125000005462 imide group Chemical group 0.000 claims description 2
- SNCZNSNPXMPCGN-UHFFFAOYSA-N butanediamide Chemical compound NC(=O)CCC(N)=O SNCZNSNPXMPCGN-UHFFFAOYSA-N 0.000 claims 2
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 claims 1
- 125000000487 histidyl group Chemical group [H]N([H])C(C(=O)O*)C([H])([H])C1=C([H])N([H])C([H])=N1 0.000 claims 1
- 125000001493 tyrosinyl group Chemical group [H]OC1=C([H])C([H])=C(C([H])=C1[H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 claims 1
- 201000011510 cancer Diseases 0.000 abstract description 13
- 235000009697 arginine Nutrition 0.000 description 35
- 210000002966 serum Anatomy 0.000 description 27
- RHGKLRLOHDJJDR-BYPYZUCNSA-N L-citrulline Chemical compound NC(=O)NCCC[C@H]([NH3+])C([O-])=O RHGKLRLOHDJJDR-BYPYZUCNSA-N 0.000 description 24
- 241000282414 Homo sapiens Species 0.000 description 23
- 229960002173 citrulline Drugs 0.000 description 23
- RHGKLRLOHDJJDR-UHFFFAOYSA-N Ndelta-carbamoyl-DL-ornithine Natural products OC(=O)C(N)CCCNC(N)=O RHGKLRLOHDJJDR-UHFFFAOYSA-N 0.000 description 22
- 235000013477 citrulline Nutrition 0.000 description 22
- 230000000694 effects Effects 0.000 description 21
- 241000699670 Mus sp. Species 0.000 description 20
- 210000004027 cell Anatomy 0.000 description 18
- 108090000623 proteins and genes Proteins 0.000 description 17
- 150000001413 amino acids Chemical group 0.000 description 16
- 241001465754 Metazoa Species 0.000 description 15
- 239000000203 mixture Substances 0.000 description 15
- 235000018102 proteins Nutrition 0.000 description 15
- 102000004169 proteins and genes Human genes 0.000 description 15
- 108090000790 Enzymes Proteins 0.000 description 13
- 102000004190 Enzymes Human genes 0.000 description 13
- 229940088598 enzyme Drugs 0.000 description 13
- 238000001727 in vivo Methods 0.000 description 9
- 235000001014 amino acid Nutrition 0.000 description 8
- 229940024606 amino acid Drugs 0.000 description 8
- 238000002474 experimental method Methods 0.000 description 8
- KQTSOJHOCCWAEH-UHFFFAOYSA-N n'-(2,5-dioxopyrrolidin-1-yl)butanediamide Chemical compound NC(=O)CCC(=O)NN1C(=O)CCC1=O KQTSOJHOCCWAEH-UHFFFAOYSA-N 0.000 description 7
- 238000002347 injection Methods 0.000 description 6
- 239000007924 injection Substances 0.000 description 6
- 238000004458 analytical method Methods 0.000 description 5
- 239000000872 buffer Substances 0.000 description 5
- 239000003153 chemical reaction reagent Substances 0.000 description 5
- MTHSVFCYNBDYFN-UHFFFAOYSA-N diethylene glycol Chemical compound OCCOCCO MTHSVFCYNBDYFN-UHFFFAOYSA-N 0.000 description 5
- 235000020776 essential amino acid Nutrition 0.000 description 5
- 239000003797 essential amino acid Substances 0.000 description 5
- 238000009472 formulation Methods 0.000 description 5
- 238000000338 in vitro Methods 0.000 description 5
- 230000004048 modification Effects 0.000 description 5
- 238000012986 modification Methods 0.000 description 5
- 241000588724 Escherichia coli Species 0.000 description 4
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 description 4
- 241000699660 Mus musculus Species 0.000 description 4
- 239000004698 Polyethylene Substances 0.000 description 4
- 230000000890 antigenic effect Effects 0.000 description 4
- 238000006243 chemical reaction Methods 0.000 description 4
- 201000010099 disease Diseases 0.000 description 4
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 4
- 231100000673 dose–response relationship Toxicity 0.000 description 4
- 238000004519 manufacturing process Methods 0.000 description 4
- 238000011580 nude mouse model Methods 0.000 description 4
- 150000003141 primary amines Chemical class 0.000 description 4
- 230000035945 sensitivity Effects 0.000 description 4
- 239000000243 solution Substances 0.000 description 4
- 239000006228 supernatant Substances 0.000 description 4
- 102100025573 1-alkyl-2-acetylglycerophosphocholine esterase Human genes 0.000 description 3
- 108010024976 Asparaginase Proteins 0.000 description 3
- 241000699666 Mus <mouse, genus> Species 0.000 description 3
- 241000589516 Pseudomonas Species 0.000 description 3
- 231100000135 cytotoxicity Toxicity 0.000 description 3
- 230000003013 cytotoxicity Effects 0.000 description 3
- 230000007423 decrease Effects 0.000 description 3
- 230000012010 growth Effects 0.000 description 3
- 210000004185 liver Anatomy 0.000 description 3
- 239000002953 phosphate buffered saline Substances 0.000 description 3
- 230000009467 reduction Effects 0.000 description 3
- 230000002829 reductive effect Effects 0.000 description 3
- 239000007787 solid Substances 0.000 description 3
- YNJBWRMUSHSURL-UHFFFAOYSA-N trichloroacetic acid Chemical compound OC(=O)C(Cl)(Cl)Cl YNJBWRMUSHSURL-UHFFFAOYSA-N 0.000 description 3
- 210000004881 tumor cell Anatomy 0.000 description 3
- 230000003442 weekly effect Effects 0.000 description 3
- KDZOASGQNOPSCU-WDSKDSINSA-N Argininosuccinic acid Chemical compound OC(=O)[C@@H](N)CCC\N=C(/N)N[C@H](C(O)=O)CC(O)=O KDZOASGQNOPSCU-WDSKDSINSA-N 0.000 description 2
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 2
- 102000003960 Ligases Human genes 0.000 description 2
- 108090000364 Ligases Proteins 0.000 description 2
- XUMBMVFBXHLACL-UHFFFAOYSA-N Melanin Chemical compound O=C1C(=O)C(C2=CNC3=C(C(C(=O)C4=C32)=O)C)=C2C4=CNC2=C1C XUMBMVFBXHLACL-UHFFFAOYSA-N 0.000 description 2
- 229920002684 Sepharose Polymers 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- 229920004890 Triton X-100 Polymers 0.000 description 2
- 239000013504 Triton X-100 Substances 0.000 description 2
- 238000002835 absorbance Methods 0.000 description 2
- OIRDTQYFTABQOQ-KQYNXXCUSA-N adenosine Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@@H]1O[C@H](CO)[C@@H](O)[C@H]1O OIRDTQYFTABQOQ-KQYNXXCUSA-N 0.000 description 2
- 125000003277 amino group Chemical group 0.000 description 2
- 230000001093 anti-cancer Effects 0.000 description 2
- 239000012131 assay buffer Substances 0.000 description 2
- 230000015572 biosynthetic process Effects 0.000 description 2
- DSEORJACOQDMQX-UHFFFAOYSA-N bis(2,3,4-trichlorophenyl) carbonate Chemical compound ClC1=C(Cl)C(Cl)=CC=C1OC(=O)OC1=CC=C(Cl)C(Cl)=C1Cl DSEORJACOQDMQX-UHFFFAOYSA-N 0.000 description 2
- 229940098773 bovine serum albumin Drugs 0.000 description 2
- 230000005907 cancer growth Effects 0.000 description 2
- PFKFTWBEEFSNDU-UHFFFAOYSA-N carbonyldiimidazole Chemical compound C1=CN=CN1C(=O)N1C=CN=C1 PFKFTWBEEFSNDU-UHFFFAOYSA-N 0.000 description 2
- 230000004087 circulation Effects 0.000 description 2
- 208000035250 cutaneous malignant susceptibility to 1 melanoma Diseases 0.000 description 2
- OPTASPLRGRRNAP-UHFFFAOYSA-N cytosine Chemical compound NC=1C=CNC(=O)N=1 OPTASPLRGRRNAP-UHFFFAOYSA-N 0.000 description 2
- 210000002889 endothelial cell Anatomy 0.000 description 2
- 230000002255 enzymatic effect Effects 0.000 description 2
- 150000002148 esters Chemical class 0.000 description 2
- 238000000855 fermentation Methods 0.000 description 2
- 230000004151 fermentation Effects 0.000 description 2
- 239000012634 fragment Substances 0.000 description 2
- 230000014509 gene expression Effects 0.000 description 2
- 230000028993 immune response Effects 0.000 description 2
- 201000010997 liver sarcoma Diseases 0.000 description 2
- 235000018977 lysine Nutrition 0.000 description 2
- 150000002669 lysines Chemical class 0.000 description 2
- 230000003211 malignant effect Effects 0.000 description 2
- 238000005259 measurement Methods 0.000 description 2
- 231100000252 nontoxic Toxicity 0.000 description 2
- 230000003000 nontoxic effect Effects 0.000 description 2
- 239000008363 phosphate buffer Substances 0.000 description 2
- 229920000573 polyethylene Polymers 0.000 description 2
- 239000002244 precipitate Substances 0.000 description 2
- 239000000047 product Substances 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 238000005215 recombination Methods 0.000 description 2
- 230000006798 recombination Effects 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 230000001225 therapeutic effect Effects 0.000 description 2
- 231100000419 toxicity Toxicity 0.000 description 2
- 230000001988 toxicity Effects 0.000 description 2
- 230000004614 tumor growth Effects 0.000 description 2
- 230000005760 tumorsuppression Effects 0.000 description 2
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 1
- 108010030844 2-methylcitrate synthase Proteins 0.000 description 1
- QFVHZQCOUORWEI-UHFFFAOYSA-N 4-[(4-anilino-5-sulfonaphthalen-1-yl)diazenyl]-5-hydroxynaphthalene-2,7-disulfonic acid Chemical compound C=12C(O)=CC(S(O)(=O)=O)=CC2=CC(S(O)(=O)=O)=CC=1N=NC(C1=CC=CC(=C11)S(O)(=O)=O)=CC=C1NC1=CC=CC=C1 QFVHZQCOUORWEI-UHFFFAOYSA-N 0.000 description 1
- 208000024893 Acute lymphoblastic leukemia Diseases 0.000 description 1
- 208000014697 Acute lymphocytic leukaemia Diseases 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
- BTBUEUYNUDRHOZ-UHFFFAOYSA-N Borate Chemical compound [O-]B([O-])[O-] BTBUEUYNUDRHOZ-UHFFFAOYSA-N 0.000 description 1
- 239000002126 C01EB10 - Adenosine Substances 0.000 description 1
- 241000511343 Chondrostoma nasus Species 0.000 description 1
- 108010071536 Citrate (Si)-synthase Proteins 0.000 description 1
- 102000006732 Citrate synthase Human genes 0.000 description 1
- 108020004705 Codon Proteins 0.000 description 1
- XFXPMWWXUTWYJX-UHFFFAOYSA-N Cyanide Chemical compound N#[C-] XFXPMWWXUTWYJX-UHFFFAOYSA-N 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
- 238000002965 ELISA Methods 0.000 description 1
- 239000004593 Epoxy Substances 0.000 description 1
- 108090000371 Esterases Proteins 0.000 description 1
- 102000001554 Hemoglobins Human genes 0.000 description 1
- 108010054147 Hemoglobins Proteins 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 1
- ODKSFYDXXFIFQN-BYPYZUCNSA-N L-arginine Chemical compound OC(=O)[C@@H](N)CCCN=C(N)N ODKSFYDXXFIFQN-BYPYZUCNSA-N 0.000 description 1
- 229930064664 L-arginine Natural products 0.000 description 1
- 235000014852 L-arginine Nutrition 0.000 description 1
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 1
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 1
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 1
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 1
- 108090000856 Lyases Proteins 0.000 description 1
- 102000004317 Lyases Human genes 0.000 description 1
- 241000124008 Mammalia Species 0.000 description 1
- 241001430197 Mollicutes Species 0.000 description 1
- 241001529936 Murinae Species 0.000 description 1
- 206010029488 Nodular melanoma Diseases 0.000 description 1
- 238000000636 Northern blotting Methods 0.000 description 1
- 108091028043 Nucleic acid sequence Proteins 0.000 description 1
- 108091034117 Oligonucleotide Proteins 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- OAICVXFJPJFONN-UHFFFAOYSA-N Phosphorus Chemical compound [P] OAICVXFJPJFONN-UHFFFAOYSA-N 0.000 description 1
- 239000004721 Polyphenylene oxide Substances 0.000 description 1
- 208000006664 Precursor Cell Lymphoblastic Leukemia-Lymphoma Diseases 0.000 description 1
- 241000555745 Sciuridae Species 0.000 description 1
- 238000012300 Sequence Analysis Methods 0.000 description 1
- 206010042553 Superficial spreading melanoma stage unspecified Diseases 0.000 description 1
- 102000019197 Superoxide Dismutase Human genes 0.000 description 1
- 108010012715 Superoxide dismutase Proteins 0.000 description 1
- 108020005038 Terminator Codon Proteins 0.000 description 1
- GLNADSQYFUSGOU-GPTZEZBUSA-J Trypan blue Chemical compound [Na+].[Na+].[Na+].[Na+].C1=C(S([O-])(=O)=O)C=C2C=C(S([O-])(=O)=O)C(/N=N/C3=CC=C(C=C3C)C=3C=C(C(=CC=3)\N=N\C=3C(=CC4=CC(=CC(N)=C4C=3O)S([O-])(=O)=O)S([O-])(=O)=O)C)=C(O)C2=C1N GLNADSQYFUSGOU-GPTZEZBUSA-J 0.000 description 1
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 1
- 108010092464 Urate Oxidase Proteins 0.000 description 1
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 1
- 229960005305 adenosine Drugs 0.000 description 1
- 125000003172 aldehyde group Chemical group 0.000 description 1
- 210000002255 anal canal Anatomy 0.000 description 1
- 150000001483 arginine derivatives Chemical class 0.000 description 1
- 229960003272 asparaginase Drugs 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-M asparaginate Chemical compound [O-]C(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-M 0.000 description 1
- 235000009582 asparagine Nutrition 0.000 description 1
- 229960001230 asparagine Drugs 0.000 description 1
- 230000002238 attenuated effect Effects 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- 230000008827 biological function Effects 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 230000017531 blood circulation Effects 0.000 description 1
- 239000001045 blue dye Substances 0.000 description 1
- 239000007853 buffer solution Substances 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- 238000007385 chemical modification Methods 0.000 description 1
- 239000007795 chemical reaction product Substances 0.000 description 1
- 239000007979 citrate buffer Substances 0.000 description 1
- 238000004440 column chromatography Methods 0.000 description 1
- 239000002299 complementary DNA Substances 0.000 description 1
- 238000009833 condensation Methods 0.000 description 1
- 230000005494 condensation Effects 0.000 description 1
- 230000021615 conjugation Effects 0.000 description 1
- 210000000795 conjunctiva Anatomy 0.000 description 1
- 230000008878 coupling Effects 0.000 description 1
- 238000010168 coupling process Methods 0.000 description 1
- 238000005859 coupling reaction Methods 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 229940104302 cytosine Drugs 0.000 description 1
- 230000002950 deficient Effects 0.000 description 1
- 230000000593 degrading effect Effects 0.000 description 1
- 239000013578 denaturing buffer Substances 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 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 description 1
- 230000008034 disappearance Effects 0.000 description 1
- 238000006073 displacement reaction Methods 0.000 description 1
- 210000002919 epithelial cell Anatomy 0.000 description 1
- 210000003238 esophagus Anatomy 0.000 description 1
- RTZKZFJDLAIYFH-UHFFFAOYSA-N ether Substances CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 1
- 239000013613 expression plasmid Substances 0.000 description 1
- 210000002950 fibroblast Anatomy 0.000 description 1
- 239000010419 fine particle Substances 0.000 description 1
- 229960004198 guanidine Drugs 0.000 description 1
- PJJJBBJSCAKJQF-UHFFFAOYSA-N guanidinium chloride Chemical compound [Cl-].NC(N)=[NH2+] PJJJBBJSCAKJQF-UHFFFAOYSA-N 0.000 description 1
- 208000006454 hepatitis Diseases 0.000 description 1
- 231100000283 hepatitis Toxicity 0.000 description 1
- 206010073071 hepatocellular carcinoma Diseases 0.000 description 1
- 231100000844 hepatocellular carcinoma Toxicity 0.000 description 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
- 239000012510 hollow fiber Substances 0.000 description 1
- 230000002163 immunogen Effects 0.000 description 1
- 230000016784 immunoglobulin production Effects 0.000 description 1
- 210000003000 inclusion body Anatomy 0.000 description 1
- 238000001361 intraarterial administration Methods 0.000 description 1
- 238000007918 intramuscular administration Methods 0.000 description 1
- 238000007912 intraperitoneal administration Methods 0.000 description 1
- 230000002601 intratumoral effect Effects 0.000 description 1
- 238000001990 intravenous administration Methods 0.000 description 1
- 238000010253 intravenous injection Methods 0.000 description 1
- IQPQWNKOIGAROB-UHFFFAOYSA-N isocyanate group Chemical group [N-]=C=O IQPQWNKOIGAROB-UHFFFAOYSA-N 0.000 description 1
- 230000002147 killing effect Effects 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 239000012669 liquid formulation Substances 0.000 description 1
- 210000004072 lung Anatomy 0.000 description 1
- 230000001926 lymphatic effect Effects 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 210000002752 melanocyte Anatomy 0.000 description 1
- 108020004999 messenger RNA Proteins 0.000 description 1
- 230000002503 metabolic effect Effects 0.000 description 1
- 230000001394 metastastic effect Effects 0.000 description 1
- 206010061289 metastatic neoplasm Diseases 0.000 description 1
- MYWUZJCMWCOHBA-VIFPVBQESA-N methamphetamine Chemical compound CN[C@@H](C)CC1=CC=CC=C1 MYWUZJCMWCOHBA-VIFPVBQESA-N 0.000 description 1
- 102000035118 modified proteins Human genes 0.000 description 1
- 108091005573 modified proteins Proteins 0.000 description 1
- 210000000214 mouth Anatomy 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- OKXGHXHZNCJMSV-UHFFFAOYSA-N nitro phenyl carbonate Chemical compound [O-][N+](=O)OC(=O)OC1=CC=CC=C1 OKXGHXHZNCJMSV-UHFFFAOYSA-N 0.000 description 1
- 125000006501 nitrophenyl group Chemical group 0.000 description 1
- 201000000032 nodular malignant melanoma Diseases 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 239000008188 pellet Substances 0.000 description 1
- 102000013415 peroxidase activity proteins Human genes 0.000 description 1
- 108040007629 peroxidase activity proteins Proteins 0.000 description 1
- 229910052698 phosphorus Inorganic materials 0.000 description 1
- 239000011574 phosphorus Substances 0.000 description 1
- 229920000728 polyester Polymers 0.000 description 1
- 229920000570 polyether Polymers 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 238000003752 polymerase chain reaction Methods 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
- 230000008569 process Effects 0.000 description 1
- 238000002731 protein assay Methods 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 230000008929 regeneration Effects 0.000 description 1
- 238000011069 regeneration method Methods 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 239000000523 sample Substances 0.000 description 1
- 239000013049 sediment Substances 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 230000001568 sexual effect Effects 0.000 description 1
- 238000002741 site-directed mutagenesis Methods 0.000 description 1
- 210000003491 skin Anatomy 0.000 description 1
- 210000000329 smooth muscle myocyte Anatomy 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 208000011584 spitz nevus Diseases 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 238000007920 subcutaneous administration Methods 0.000 description 1
- KDYFGRWQOYBRFD-UHFFFAOYSA-L succinate(2-) Chemical compound [O-]C(=O)CCC([O-])=O KDYFGRWQOYBRFD-UHFFFAOYSA-L 0.000 description 1
- 150000003457 sulfones Chemical class 0.000 description 1
- 208000030457 superficial spreading melanoma Diseases 0.000 description 1
- 230000004083 survival effect Effects 0.000 description 1
- 210000001179 synovial fluid Anatomy 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 238000002560 therapeutic procedure Methods 0.000 description 1
- 125000003396 thiol group Chemical group [H]S* 0.000 description 1
- 150000003573 thiols Chemical class 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 231100000331 toxic Toxicity 0.000 description 1
- 231100000167 toxic agent Toxicity 0.000 description 1
- 230000002588 toxic effect Effects 0.000 description 1
- 239000003440 toxic substance Substances 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
- 231100000402 unacceptable toxicity Toxicity 0.000 description 1
- 210000001215 vagina Anatomy 0.000 description 1
- 230000035899 viability Effects 0.000 description 1
- 125000000391 vinyl group Chemical group [H]C([*])=C([H])[H] 0.000 description 1
- 229920002554 vinyl polymer Polymers 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-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
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/96—Stabilising an enzyme by forming an adduct or a composition; Forming enzyme conjugates
-
- 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
- A61K38/43—Enzymes; Proenzymes; Derivatives thereof
- A61K38/46—Hydrolases (3)
- A61K38/50—Hydrolases (3) acting on carbon-nitrogen bonds, other than peptide bonds (3.5), e.g. asparaginase
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K47/00—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient
- A61K47/50—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates
- A61K47/51—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent
- A61K47/56—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being an organic macromolecular compound, e.g. an oligomeric, polymeric or dendrimeric molecule
- A61K47/59—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being an organic macromolecular compound, e.g. an oligomeric, polymeric or dendrimeric molecule obtained otherwise than by reactions only involving carbon-to-carbon unsaturated bonds, e.g. polyureas or polyurethanes
- A61K47/60—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being an organic macromolecular compound, e.g. an oligomeric, polymeric or dendrimeric molecule obtained otherwise than by reactions only involving carbon-to-carbon unsaturated bonds, e.g. polyureas or polyurethanes the organic macromolecular compound being a polyoxyalkylene oligomer, polymer or dendrimer, e.g. PEG, PPG, PEO or polyglycerol
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
-
- 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
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/78—Hydrolases (3) acting on carbon to nitrogen bonds other than peptide bonds (3.5)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y305/00—Hydrolases acting on carbon-nitrogen bonds, other than peptide bonds (3.5)
- C12Y305/03—Hydrolases acting on carbon-nitrogen bonds, other than peptide bonds (3.5) in linear amidines (3.5.3)
- C12Y305/03006—Arginine deiminase (3.5.3.6)
-
- 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
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02A—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE
- Y02A50/00—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE in human health protection, e.g. against extreme weather
- Y02A50/30—Against vector-borne diseases, e.g. mosquito-borne, fly-borne, tick-borne or waterborne diseases whose impact is exacerbated by climate change
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Wood Science & Technology (AREA)
- Zoology (AREA)
- Medicinal Chemistry (AREA)
- Biochemistry (AREA)
- General Engineering & Computer Science (AREA)
- Veterinary Medicine (AREA)
- Animal Behavior & Ethology (AREA)
- Pharmacology & Pharmacy (AREA)
- Public Health (AREA)
- Biotechnology (AREA)
- Biomedical Technology (AREA)
- Molecular Biology (AREA)
- Microbiology (AREA)
- Epidemiology (AREA)
- Immunology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Gastroenterology & Hepatology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Enzymes And Modification Thereof (AREA)
- Medicinal Preparation (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Chemical Or Physical Treatment Of Fibers (AREA)
Abstract
Description
Claims (1)
- 【特許請求の範囲】 1. ポリエチレングリコールに連結基を介して共有結合したアルギニンデイ ミナーゼを含んでなり、かつ、ここにおいて、ポリエチレングリコールが約12 ,000〜約40,000の範囲の全重量平均分子量を有する化合物。 2. 該連結基がマレイミド基である、請求の範囲1の化合物。 3. 該マレイミド基がスクシンイミジルスクシネート、スクシンイミジルプロ ピオネート、スクシンイミジルカルボキシメチレート、スクシンイミジルスクシ ンアミド、N−ヒドロキシスクシンイミドまたはそれらの組み合わせである、請 求の範囲2の化合物。 4. 該マレイミド基がスクシンイミジルスクシネート、スクシンイミジルプ ロピオネートまたはそれらの組み合わせである、請求の範囲3の化合物。 5. 該アルギニンデイミナーゼがマイコプラズマ属の微生物から得られる、 請求の範囲1の化合物。 6. 該微生物がマイコプラズマ・アルギニニ、マイコプラズマ・ホミナス、 マイコプラズマ・アルトリチデス及びそれらの組み合わせよりなる群から選択さ れる、請求の範囲5の化合物。 7. 該アルギニンデイミナーゼが約7〜約15のポリエチレングリコール分 子に共有結合している、請求の範囲1の化合物。 8. 該アルギニンデイミナーゼが約9〜約12のポリエチレングリコール分 子に共有結合している、請求の範囲7の化合物。 9. 該ポリエチレングリコールが約12,000から約30,000までの 全重量平均分子量を有する、請求の範囲1の化合物。 10. ポリエチレングリコールに連結基を介してアルギニンデイミナーゼを 共有結合することにより該アルギニンデイミナーゼを修飾することを含んでなる アルギニンデイミナーゼの循環半減期を増大する方法であって、ここで、ポリエ チレングリコールが約12,000から約40,000までの範囲の全重量平均 分子量を有する方法。 11. 請求の範囲1の化合物の治療的に有効な量を患者に投与することを含 んでなる該患者における腫瘍の処置方法。 12. 該腫瘍が黒色腫である、請求の範囲11の方法。 13. 該ポリエチレングリコールが約20,000の全重量平均分子量を有 する、請求の範囲12の方法。 14. 該連結基がマレイミド基である、請求の範囲12の方法。 15. 該マレイミド基がスクシンイミジルスクシネート、スクシンイミジル プロピオネート、スクシンイミジルカルボキシメチレート、スクシンイミジルス クシンアミド、N−ヒドロキシスクシンイミドまたはそれらの組み合わせである 、請求の範囲14の方法。 16. ポリエチレングリコールに連結基を介して共有結合したアルギニンデ イミナーゼを含んでなる化合物の治療的に有効な量を患者に投与することを含ん でなる該患者における肝臓癌の処置方法であって、ここで、ポリエチレングリコ ールが約5,000の範囲の全重量平均分子量を有する方法。 17. 該連結基がマレイミド基である、請求の範囲16の方法。 18. 該マレイミド基がスクシンイミジルスクシネート、スクシンイミジル プロピオネート、スクシンイミジルカルボキシメチレート、スクシンイミジルス クシンアミド、N−ヒドロキシスクシンイミドまたは それらの組み合わせである、請求の範囲17の方法。 19. 該腫瘍が肉腫である請求の範囲11の方法。 20. 請求の範囲1の化合物の治療的に有効な量を患者に投与することを含 んでなる該患者における転移の処置及び抑制方法。 21. ポリエチレングリコールに連結基を介して共有結合したアルギニンデ イミナーゼを含んでなり、かつポリエチレングリコールが約1,000から約4 0,000までの全重量平均分子量を有し、そして連結基がマレイミド基、アミ ド基、イミド基、カルバメート基、エステル基、エポキシ基、カルボキシル基、 ヒドロキシル基、炭水化物、チロシン基、システイン基、ヒスチジン基及びそれ らの組み合わせよりなる群から選択される化合物。
Applications Claiming Priority (5)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US4620097P | 1997-05-12 | 1997-05-12 | |
US60/046,200 | 1997-05-12 | ||
US09/023,809 | 1998-02-13 | ||
US09/023,809 US6183738B1 (en) | 1997-05-12 | 1998-02-13 | Modified arginine deiminase |
PCT/US1998/009575 WO1998051784A1 (en) | 1997-05-12 | 1998-05-12 | Modiified arginine deiminase |
Publications (3)
Publication Number | Publication Date |
---|---|
JP2001524836A true JP2001524836A (ja) | 2001-12-04 |
JP2001524836A5 JP2001524836A5 (ja) | 2005-12-02 |
JP4456184B2 JP4456184B2 (ja) | 2010-04-28 |
Family
ID=26697638
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP54937598A Expired - Lifetime JP4456184B2 (ja) | 1997-05-12 | 1998-05-12 | 修飾されたアルギニンデイミナーゼ |
Country Status (14)
Country | Link |
---|---|
US (3) | US6183738B1 (ja) |
EP (1) | EP0981607B1 (ja) |
JP (1) | JP4456184B2 (ja) |
CN (1) | CN1169951C (ja) |
AT (1) | ATE335814T1 (ja) |
AU (1) | AU724907B2 (ja) |
CA (1) | CA2288948C (ja) |
CY (1) | CY1105758T1 (ja) |
DE (1) | DE69835515T2 (ja) |
DK (1) | DK0981607T3 (ja) |
ES (1) | ES2270515T3 (ja) |
PT (1) | PT981607E (ja) |
TW (1) | TW368504B (ja) |
WO (1) | WO1998051784A1 (ja) |
Cited By (4)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JP2014521602A (ja) * | 2012-04-04 | 2014-08-28 | ポラリス グループ | アルギニンデイミナーゼを用いる処置方法 |
JP2016519069A (ja) * | 2013-03-15 | 2016-06-30 | ポラリス グループ | 癌治療のためのadi−peg20抗体に対して低減された交差反応性を有するアルギニンデイミナーゼ |
JP2017513516A (ja) * | 2014-03-18 | 2017-06-01 | ティーディーダブリュ グループTdw Group | 操作されたキメラpeg化adi及び使用方法 |
US9789170B2 (en) | 2014-09-16 | 2017-10-17 | Polaris Group | Arginine deiminase with reduced cross-reactivity toward ADI-PEG 20 antibodies for cancer treatment |
Families Citing this family (109)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US5545553A (en) * | 1994-09-26 | 1996-08-13 | The Rockefeller University | Glycosyltransferases for biosynthesis of oligosaccharides, and genes encoding them |
US6183738B1 (en) | 1997-05-12 | 2001-02-06 | Phoenix Pharamacologics, Inc. | Modified arginine deiminase |
US6635462B1 (en) * | 1997-05-12 | 2003-10-21 | Phoenix Pharmacologies, Inc. | Mutated form of arginine deiminase |
US5985263A (en) * | 1997-12-19 | 1999-11-16 | Enzon, Inc. | Substantially pure histidine-linked protein polymer conjugates |
CN1328152A (zh) * | 2000-06-14 | 2001-12-26 | 上海博德基因开发有限公司 | 一种新的多肽——人nrd转化酶10.01和编码这种多肽的多核苷酸 |
US20040096437A1 (en) * | 2000-07-27 | 2004-05-20 | Bon-Hong Min | Pharmaceutical composition comprising arginine deiminasa for inhibiting angio-genesis |
WO2002009741A1 (en) * | 2000-07-27 | 2002-02-07 | Angiolab, Inc. | The pharmaceutical composition comprising arginine deiminase for inhibiting angiogenesis |
JP2004515232A (ja) * | 2000-11-28 | 2004-05-27 | フエニツクス・フアーマコロジクス・インコーポレーテツド | 修飾されたアルギニンデイミナーゼ |
US20050063942A1 (en) * | 2001-02-02 | 2005-03-24 | Clark Mike A. | Methods for predicting sensitivity of tumors to arginine deprivation |
US7795210B2 (en) * | 2001-10-10 | 2010-09-14 | Novo Nordisk A/S | Protein remodeling methods and proteins/peptides produced by the methods |
US7265084B2 (en) * | 2001-10-10 | 2007-09-04 | Neose Technologies, Inc. | Glycopegylation methods and proteins/peptides produced by the methods |
US7173003B2 (en) * | 2001-10-10 | 2007-02-06 | Neose Technologies, Inc. | Granulocyte colony stimulating factor: remodeling and glycoconjugation of G-CSF |
US7157277B2 (en) | 2001-11-28 | 2007-01-02 | Neose Technologies, Inc. | Factor VIII remodeling and glycoconjugation of Factor VIII |
US7399613B2 (en) * | 2001-10-10 | 2008-07-15 | Neose Technologies, Inc. | Sialic acid nucleotide sugars |
US7696163B2 (en) * | 2001-10-10 | 2010-04-13 | Novo Nordisk A/S | Erythropoietin: remodeling and glycoconjugation of erythropoietin |
US7214660B2 (en) * | 2001-10-10 | 2007-05-08 | Neose Technologies, Inc. | Erythropoietin: remodeling and glycoconjugation of erythropoietin |
US8008252B2 (en) * | 2001-10-10 | 2011-08-30 | Novo Nordisk A/S | Factor VII: remodeling and glycoconjugation of Factor VII |
ES2516041T3 (es) * | 2001-10-10 | 2014-10-30 | Ratiopharm Gmbh | Remodelación y glicoconjugación de la hormona del crecimiento humano (hGH) |
US7179617B2 (en) * | 2001-10-10 | 2007-02-20 | Neose Technologies, Inc. | Factor IX: remolding and glycoconjugation of Factor IX |
US7473680B2 (en) | 2001-11-28 | 2009-01-06 | Neose Technologies, Inc. | Remodeling and glycoconjugation of peptides |
DE60336555D1 (de) * | 2002-06-21 | 2011-05-12 | Novo Nordisk Healthcare Ag | Pegylierte glykoformen von faktor vii |
CN100405906C (zh) * | 2002-10-09 | 2008-07-30 | 尼奥斯技术有限公司 | 促红细胞生成素:促红细胞生成素的重构和糖缀合 |
CN1809378B (zh) * | 2002-11-18 | 2010-06-23 | 德西涅Rx制药公司 | 体内抑制病毒复制的方法 |
US7432331B2 (en) * | 2002-12-31 | 2008-10-07 | Nektar Therapeutics Al, Corporation | Hydrolytically stable maleimide-terminated polymers |
AU2003300133B2 (en) * | 2002-12-31 | 2008-11-13 | Nektar Therapeutics | Hydrolytically stable maleimide-terminated polymers |
ATE399185T1 (de) * | 2002-12-31 | 2008-07-15 | Nektar Therapeutics Al Corp | Maleinsäureamid polymerderivate und ihre biokonjugate |
KR20060003862A (ko) * | 2003-03-14 | 2006-01-11 | 네오스 테크놀로지스, 인크. | 수용성분기폴리머 및 그 접합체 |
US8791070B2 (en) | 2003-04-09 | 2014-07-29 | Novo Nordisk A/S | Glycopegylated factor IX |
MXPA05010773A (es) * | 2003-04-09 | 2005-12-12 | Neose Technologies Inc | Metodos de glicopegilacion y proteinas/peptidos producidos por los metodos. |
EP1613261A4 (en) * | 2003-04-09 | 2011-01-26 | Novo Nordisk As | INTRA-CELLULAR FORMATION OF PEPTIDE CONJUGATES |
CN100522988C (zh) * | 2003-04-09 | 2009-08-05 | 诺和诺德公司 | 糖peg化方法及由该方法生产的蛋白质/肽 |
EP1624847B1 (en) | 2003-05-09 | 2012-01-04 | BioGeneriX AG | Compositions and methods for the preparation of human growth hormone glycosylation mutants |
WO2005012484A2 (en) | 2003-07-25 | 2005-02-10 | Neose Technologies, Inc. | Antibody-toxin conjugates |
AU2004293103C1 (en) * | 2003-11-24 | 2010-12-02 | Ratiopharm Gmbh | Glycopegylated erythropoietin |
US8633157B2 (en) * | 2003-11-24 | 2014-01-21 | Novo Nordisk A/S | Glycopegylated erythropoietin |
US7842661B2 (en) * | 2003-11-24 | 2010-11-30 | Novo Nordisk A/S | Glycopegylated erythropoietin formulations |
US20080305992A1 (en) * | 2003-11-24 | 2008-12-11 | Neose Technologies, Inc. | Glycopegylated erythropoietin |
KR101237884B1 (ko) * | 2003-12-03 | 2013-02-27 | 바이오제너릭스 에이지 | 글리코 peg화 과립구 콜로니 자극인자 |
US20080318850A1 (en) * | 2003-12-03 | 2008-12-25 | Neose Technologies, Inc. | Glycopegylated Factor Ix |
US20060040856A1 (en) | 2003-12-03 | 2006-02-23 | Neose Technologies, Inc. | Glycopegylated factor IX |
US7956032B2 (en) * | 2003-12-03 | 2011-06-07 | Novo Nordisk A/S | Glycopegylated granulocyte colony stimulating factor |
AU2004297228A1 (en) | 2003-12-03 | 2005-06-23 | Nektar Therapeutics Al, Corporation | Method of preparing maleimide functionalized polymers |
BRPI0506741A (pt) * | 2004-01-08 | 2007-05-15 | Neose Technologies Inc | glicosilação de peptìdeos ligados a o |
US9085659B2 (en) | 2004-05-03 | 2015-07-21 | Nektar Therapeutics | Polymer derivatives comprising an imide branching point |
BRPI0510295A (pt) | 2004-05-04 | 2007-11-06 | Novo Nordisk Healthcare Ag | preparação de uma glicoproteìna, e, método para produzir a mesma |
US20080300173A1 (en) | 2004-07-13 | 2008-12-04 | Defrees Shawn | Branched Peg Remodeling and Glycosylation of Glucagon-Like Peptides-1 [Glp-1] |
CN1745847A (zh) * | 2004-09-08 | 2006-03-15 | 康达医药科技有限公司 | 用精氨酸酶治疗肝炎的药物组合物和方法 |
US8268967B2 (en) * | 2004-09-10 | 2012-09-18 | Novo Nordisk A/S | Glycopegylated interferon α |
EP1797192A1 (en) * | 2004-09-29 | 2007-06-20 | Novo Nordisk Health Care AG | Modified proteins |
JP5948627B2 (ja) | 2004-10-29 | 2016-07-20 | レイショファーム ゲーエムベーハー | 線維芽細胞成長因子(fgf)のリモデリングと糖質ペグ化 |
JP2008526864A (ja) * | 2005-01-06 | 2008-07-24 | ネオス テクノロジーズ インコーポレイテッド | 糖断片を用いる糖結合 |
EP1858543B1 (en) | 2005-01-10 | 2013-11-27 | BioGeneriX AG | Glycopegylated granulocyte colony stimulating factor |
WO2006105426A2 (en) * | 2005-03-30 | 2006-10-05 | Neose Technologies, Inc. | Manufacturing process for the production of peptides grown in insect cell lines |
US20070154992A1 (en) * | 2005-04-08 | 2007-07-05 | Neose Technologies, Inc. | Compositions and methods for the preparation of protease resistant human growth hormone glycosylation mutants |
FR2884717B1 (fr) * | 2005-04-25 | 2009-07-03 | Erytech Pharma Soc Par Actions | Erythrocytes renfermant de l'arginine deiminase |
JP5216580B2 (ja) | 2005-05-25 | 2013-06-19 | ノヴォ ノルディスク アー/エス | グリコペグ化第ix因子 |
EP1915412B1 (en) * | 2005-07-19 | 2010-03-24 | Nektar Therapeutics | Method for preparing polymer maleimides |
US20070105755A1 (en) | 2005-10-26 | 2007-05-10 | Neose Technologies, Inc. | One pot desialylation and glycopegylation of therapeutic peptides |
JP2009515508A (ja) * | 2005-08-19 | 2009-04-16 | ネオス テクノロジーズ インコーポレイテッド | グリコpeg化因子viiおよび因子viia |
US20090048440A1 (en) * | 2005-11-03 | 2009-02-19 | Neose Technologies, Inc. | Nucleotide Sugar Purification Using Membranes |
CN101002945B (zh) * | 2006-01-20 | 2012-09-05 | 清华大学 | 一种用于肿瘤治疗的新型复合物 |
AU2007245190B2 (en) | 2006-03-31 | 2011-07-21 | Takeda Pharmaceutical Company Limited | Pegylated factor VIII |
US7985839B2 (en) * | 2006-03-31 | 2011-07-26 | Baxter International Inc. | Factor VIII polymer conjugates |
US7645860B2 (en) * | 2006-03-31 | 2010-01-12 | Baxter Healthcare S.A. | Factor VIII polymer conjugates |
US7982010B2 (en) * | 2006-03-31 | 2011-07-19 | Baxter International Inc. | Factor VIII polymer conjugates |
US7534595B2 (en) * | 2006-06-12 | 2009-05-19 | Biomarin Pharmaceutical Inc. | Compositions of prokaryotic phenylalanine ammonia-lyase and methods of using compositions thereof |
US7531341B1 (en) | 2006-06-12 | 2009-05-12 | Biomarin Pharmaceutical Inc. | Compositions of prokaryotic phenylalanine ammonia-lyase and methods of using compositions thereof |
CN101516388B (zh) * | 2006-07-21 | 2012-10-31 | 诺和诺德公司 | 通过o-联糖基化序列的肽的糖基化 |
EP2054521A4 (en) * | 2006-10-03 | 2012-12-19 | Novo Nordisk As | METHODS OF PURIFYING CONJUGATES OF POLYPEPTIDES |
KR101556248B1 (ko) * | 2006-10-04 | 2015-09-30 | 노보 노르디스크 에이/에스 | 글리세롤이 연결된 페길화된 당 및 글리코펩티드 |
WO2008073620A2 (en) * | 2006-11-02 | 2008-06-19 | Neose Technologies, Inc. | Manufacturing process for the production of polypeptides expressed in insect cell-lines |
ES2521490T3 (es) | 2006-12-15 | 2014-11-12 | Baxter International Inc. | Conjugado de factor VIIa - ácido (poli)siálico con una vida media in vivo prolongada. |
RS52845B (en) * | 2007-04-03 | 2013-12-31 | Biogenerix Ag | TREATMENT PROCEDURES USING GLYCOPEGILATED G-CSF |
US20090053167A1 (en) * | 2007-05-14 | 2009-02-26 | Neose Technologies, Inc. | C-, S- and N-glycosylation of peptides |
US20080292609A1 (en) * | 2007-05-21 | 2008-11-27 | Ning Man Cheng | Use of Arginase in Combination with 5FU and Other Compounds for Treatment of Human Malignancies |
JP2010531135A (ja) * | 2007-06-04 | 2010-09-24 | ノボ ノルディスク アクティーゼルスカブ | N−アセチルグルコサミニルトランスフェラーゼを使用したo結合型グリコシル化 |
US9493499B2 (en) * | 2007-06-12 | 2016-11-15 | Novo Nordisk A/S | Process for the production of purified cytidinemonophosphate-sialic acid-polyalkylene oxide (CMP-SA-PEG) as modified nucleotide sugars via anion exchange chromatography |
FR2919804B1 (fr) | 2007-08-08 | 2010-08-27 | Erytech Pharma | Composition et vaccin therapeutique anti-tumoral |
US7537923B2 (en) * | 2007-08-17 | 2009-05-26 | Biomarin Pharmaceutical Inc. | Compositions of prokaryotic phenylalanine ammonia-lyase and methods of treating cancer using compositions thereof |
US8207112B2 (en) * | 2007-08-29 | 2012-06-26 | Biogenerix Ag | Liquid formulation of G-CSF conjugate |
JP5647899B2 (ja) * | 2008-01-08 | 2015-01-07 | ラツィオファルム ゲーエムベーハーratiopharm GmbH | オリゴサッカリルトランスフェラーゼを使用するポリペプチドの複合糖質化 |
EP2257311B1 (en) | 2008-02-27 | 2014-04-16 | Novo Nordisk A/S | Conjugated factor viii molecules |
WO2010014225A2 (en) | 2008-07-30 | 2010-02-04 | Biomarin Pharmaceutical Inc. | Assays for detection of phenylalanine ammonia-lyase and antibodies to phenylalanine ammonia-lyase |
WO2010023195A2 (en) | 2008-08-26 | 2010-03-04 | Kyon Biotech Ag | Compositions and methods for treating cancer |
US20100150949A1 (en) * | 2008-12-16 | 2010-06-17 | Oncopharmacologics, Inc. | Methods and compositions for modulating proline levels |
US8642737B2 (en) | 2010-07-26 | 2014-02-04 | Baxter International Inc. | Nucleophilic catalysts for oxime linkage |
US8809501B2 (en) | 2009-07-27 | 2014-08-19 | Baxter International Inc. | Nucleophilic catalysts for oxime linkage |
WO2011017055A2 (en) * | 2009-07-27 | 2011-02-10 | Baxter International Inc. | Blood coagulation protein conjugates |
ES2590679T3 (es) | 2009-07-27 | 2016-11-23 | Lipoxen Technologies Limited | Glicopolisialilación de proteínas diferentes a proteínas de coagulación de la sangre |
EP3093029A1 (en) | 2009-07-27 | 2016-11-16 | Baxalta GmbH | Blood coagulation protein conjugates |
EP2295560A1 (en) | 2009-09-14 | 2011-03-16 | RWTH Aachen University | Directed evolution of arginine deiminase for increased activity at physiological pH |
EP3025728B1 (en) | 2010-02-04 | 2018-08-08 | BioMarin Pharmaceutical Inc. | Method for purifying prokaryotic phenylalanine ammonia-lyase variants |
CN101812438B (zh) * | 2010-03-25 | 2014-08-27 | 江苏泰康生物医药有限公司 | 一种精氨酸脱亚氨酶突变体及其制备与应用 |
WO2012075173A2 (en) | 2010-12-01 | 2012-06-07 | Board Of Regents The University Of Texas System | Compositions and method for deimmunization of proteins |
MX345608B (es) | 2010-12-22 | 2017-02-07 | Baxalta Inc | Materiales y metodos para conjugar un derivado de acido graso soluble en agua a una proteina. |
WO2014001956A2 (en) * | 2012-06-25 | 2014-01-03 | Ning Man Cheng | Combinational use of pegylated recombinant human arginase with chemotherapeutic/target therapeutic drug in cancer treatment |
USRE48805E1 (en) | 2013-03-06 | 2021-11-02 | Vision Global Holdings Ltd. | Method for cancer targeting treatment and detection of arginine using albumin-binding arginine deiminase fusion protein |
US9255262B2 (en) | 2013-03-06 | 2016-02-09 | Vision Global Holdings Ltd. | Albumin-binding arginine deminase and the use thereof |
WO2015051340A1 (en) | 2013-10-04 | 2015-04-09 | Ann David K | Methods for treating breast and other cancers by targeting argininosuccinate synthetase 1-deficiency |
TWI676683B (zh) * | 2014-03-14 | 2019-11-11 | 開曼群島商瑞華藥業集團 | 用於癌症治療之對adi-peg20抗體交叉反應性降低之精胺酸去亞胺酶 |
CN103923898A (zh) * | 2014-04-17 | 2014-07-16 | 江南大学 | 一种peg修饰的重组精氨酸脱亚胺酶及其制备方法和应用 |
EP3166972B1 (en) | 2014-07-08 | 2020-03-11 | TDW Group | Antibodies to argininosuccinate synthase and related methods |
CN104726478A (zh) * | 2015-03-09 | 2015-06-24 | 武汉远大弘元股份有限公司 | 表达精氨酸脱亚胺酶基因的重组大肠杆菌及其应用 |
WO2017041051A1 (en) | 2015-09-04 | 2017-03-09 | Sqz Biotechnologies Company | Intracellular delivery of biomolecules to cells comprising a cell wall |
US20180296652A1 (en) * | 2016-11-02 | 2018-10-18 | Polaris Group | Formulations of pegylated arginine deiminase |
CN106591271B (zh) * | 2017-03-02 | 2019-07-16 | 江南大学 | 一株酶活和温度稳定性提高的精氨酸脱亚胺酶突变体及其应用 |
WO2019042628A1 (en) | 2017-08-31 | 2019-03-07 | Erytech Pharma | ARGININE DEIMINASE ENCAPSULATED WITHIN ERYTHROCYTES AND THEIR USE IN THE TREATMENT OF CANCER AND ARGINASE-1 DEFICIENCY |
EP3449935A1 (en) | 2017-08-31 | 2019-03-06 | Erytech Pharma | Arginine deiminase encapsulated inside erythrocytes and their use in treating cancer and arginase-1 deficiency |
CN112513099A (zh) * | 2018-05-31 | 2021-03-16 | 香港理工大学 | 用于癌症、肥胖症、代谢紊乱和相关并发症及合并症的精氨酸耗竭剂的组合物和应用 |
Family Cites Families (17)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US4179337A (en) | 1973-07-20 | 1979-12-18 | Davis Frank F | Non-immunogenic polypeptides |
US4609546A (en) | 1982-06-24 | 1986-09-02 | Japan Chemical Research Co., Ltd. | Long-acting composition |
US5447722A (en) | 1983-12-12 | 1995-09-05 | University Of Manitoba | Method for the suppression of an immune response with antigen-MPEG conjugates in nonsensitized individuals |
EP0230777B1 (en) * | 1985-12-28 | 1991-04-10 | Ohgen Research Laboratories Ltd., | Antitumor protein gene of streptococcus pyogenes su, plasmids containing the gene, transformant cells harboring the plasmids, and process for producing the antitumor protein |
US5080891A (en) | 1987-08-03 | 1992-01-14 | Ddi Pharmaceuticals, Inc. | Conjugates of superoxide dismutase coupled to high molecular weight polyalkylene glycols |
JPH0253490A (ja) | 1988-08-16 | 1990-02-22 | Agency Of Ind Science & Technol | アルギニン・デイミナーゼ遺伝子 |
WO1990005534A1 (en) | 1988-11-23 | 1990-05-31 | Genentech, Inc. | Polypeptide derivatives |
JP2900279B2 (ja) | 1989-08-02 | 1999-06-02 | 株式会社ジャパンエナジー | 新規なアルギニンデイミナーゼ、その製造法及び該酵素を有効成分とする制癌剤 |
JP2736145B2 (ja) | 1990-01-11 | 1998-04-02 | 関東電化工業株式会社 | パーハロゲン化エチレンの製造法 |
JPH04218000A (ja) * | 1990-02-13 | 1992-08-07 | Kirin Amgen Inc | 修飾ポリペプチド |
JP3209338B2 (ja) | 1990-09-10 | 2001-09-17 | 株式会社ジャパンエナジー | ポリエチレングリコール修飾アルギニンデイミナーゼおよびその製造法 |
US5372942A (en) * | 1992-02-10 | 1994-12-13 | Coriell Institute For Medical Research | Protease K resistant arginine deiminase, its method of preparation and its use as an anti-neoplastic agent |
WO1994005332A2 (en) | 1992-09-01 | 1994-03-17 | Berlex Laboratories, Inc. | Glycolation of glycosylated macromolecules |
US5695760A (en) | 1995-04-24 | 1997-12-09 | Boehringer Inglehiem Pharmaceuticals, Inc. | Modified anti-ICAM-1 antibodies and their use in the treatment of inflammation |
US5804183A (en) | 1997-01-31 | 1998-09-08 | Enzon, Inc. | Arginine deminase derived from mycoplasma arthritidis and polymer conjugates containing the same |
US6183738B1 (en) | 1997-05-12 | 2001-02-06 | Phoenix Pharamacologics, Inc. | Modified arginine deiminase |
US6180387B1 (en) | 1997-08-11 | 2001-01-30 | Smithkline Beecham Corporation | Arginine deiminase |
-
1998
- 1998-02-13 US US09/023,809 patent/US6183738B1/en not_active Expired - Lifetime
- 1998-05-12 AU AU74798/98A patent/AU724907B2/en not_active Expired
- 1998-05-12 CN CNB988050668A patent/CN1169951C/zh not_active Expired - Lifetime
- 1998-05-12 WO PCT/US1998/009575 patent/WO1998051784A1/en active IP Right Grant
- 1998-05-12 ES ES98922197T patent/ES2270515T3/es not_active Expired - Lifetime
- 1998-05-12 TW TW087107257A patent/TW368504B/zh not_active IP Right Cessation
- 1998-05-12 PT PT98922197T patent/PT981607E/pt unknown
- 1998-05-12 AT AT98922197T patent/ATE335814T1/de active
- 1998-05-12 DE DE69835515T patent/DE69835515T2/de not_active Expired - Lifetime
- 1998-05-12 CA CA002288948A patent/CA2288948C/en not_active Expired - Lifetime
- 1998-05-12 DK DK98922197T patent/DK0981607T3/da active
- 1998-05-12 EP EP98922197A patent/EP0981607B1/en not_active Expired - Lifetime
- 1998-05-12 JP JP54937598A patent/JP4456184B2/ja not_active Expired - Lifetime
-
2000
- 2000-11-28 US US09/723,546 patent/US6737259B1/en not_active Expired - Lifetime
-
2004
- 2004-01-15 US US10/757,843 patent/US7323167B2/en not_active Expired - Lifetime
-
2006
- 2006-11-03 CY CY20061101590T patent/CY1105758T1/el unknown
Cited By (9)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JP2014521602A (ja) * | 2012-04-04 | 2014-08-28 | ポラリス グループ | アルギニンデイミナーゼを用いる処置方法 |
US9333268B2 (en) | 2012-04-04 | 2016-05-10 | Polaris Group | Methods of treatment with arginine deiminase |
US9731028B2 (en) | 2012-04-04 | 2017-08-15 | Polaris Group | Methods of treatment with arginine deiminase |
US10525142B2 (en) | 2012-04-04 | 2020-01-07 | Polaris Group | Methods of treatment with arginine deiminase |
JP2016519069A (ja) * | 2013-03-15 | 2016-06-30 | ポラリス グループ | 癌治療のためのadi−peg20抗体に対して低減された交差反応性を有するアルギニンデイミナーゼ |
US11235037B2 (en) | 2013-03-15 | 2022-02-01 | Polaris Group | Arginine deiminase with reduced cross-reactivity toward ADI - PEG 20 antibodies for cancer treatment |
JP2017513516A (ja) * | 2014-03-18 | 2017-06-01 | ティーディーダブリュ グループTdw Group | 操作されたキメラpeg化adi及び使用方法 |
US10463721B2 (en) | 2014-03-18 | 2019-11-05 | Tdw Group | Engineered chimeric pegylated ADI and methods of use |
US9789170B2 (en) | 2014-09-16 | 2017-10-17 | Polaris Group | Arginine deiminase with reduced cross-reactivity toward ADI-PEG 20 antibodies for cancer treatment |
Also Published As
Publication number | Publication date |
---|---|
US6737259B1 (en) | 2004-05-18 |
US6183738B1 (en) | 2001-02-06 |
DE69835515D1 (de) | 2006-09-21 |
CN1169951C (zh) | 2004-10-06 |
DK0981607T3 (da) | 2006-12-11 |
EP0981607A1 (en) | 2000-03-01 |
AU724907B2 (en) | 2000-10-05 |
CN1255944A (zh) | 2000-06-07 |
EP0981607A4 (en) | 2004-09-01 |
CA2288948A1 (en) | 1998-11-19 |
ES2270515T3 (es) | 2007-04-01 |
JP4456184B2 (ja) | 2010-04-28 |
PT981607E (pt) | 2006-11-30 |
ATE335814T1 (de) | 2006-09-15 |
CY1105758T1 (el) | 2010-12-22 |
DE69835515T2 (de) | 2007-08-09 |
AU7479898A (en) | 1998-12-08 |
WO1998051784A1 (en) | 1998-11-19 |
US20050129706A1 (en) | 2005-06-16 |
TW368504B (en) | 1999-09-01 |
US7323167B2 (en) | 2008-01-29 |
CA2288948C (en) | 2007-10-30 |
EP0981607B1 (en) | 2006-08-09 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
JP2001524836A (ja) | 修飾されたアルギニンデイミナーゼ | |
JP5341945B2 (ja) | 非免疫原性ポリマー結合体の調製のための凝集体非含有尿酸オキシダーゼ | |
KR101022577B1 (ko) | 항원성이 감소한 중합체 콘쥬게이트, 이의 제조방법 및용도 | |
JP2004515232A (ja) | 修飾されたアルギニンデイミナーゼ | |
JP2002522399A (ja) | Peg−尿酸酸化酵素結合体およびその使用 | |
US7452533B2 (en) | Antimicrobial polymer conjugate containing lysostaphin and polyethylene glycol | |
CN101591649B (zh) | 甲氧基聚乙二醇修饰的精氨酸脱亚氨酶及其制备与应用 |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20050509 |
|
A621 | Written request for application examination |
Free format text: JAPANESE INTERMEDIATE CODE: A621 Effective date: 20050509 |
|
A711 | Notification of change in applicant |
Free format text: JAPANESE INTERMEDIATE CODE: A711 Effective date: 20070110 |
|
A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20080729 |
|
RD02 | Notification of acceptance of power of attorney |
Free format text: JAPANESE INTERMEDIATE CODE: A7422 Effective date: 20080825 |
|
A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20081029 |
|
A602 | Written permission of extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A602 Effective date: 20081208 |
|
A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20090126 |
|
A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20090721 |
|
A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20091021 |
|
A602 | Written permission of extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A602 Effective date: 20091130 |
|
A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20091217 |
|
TRDD | Decision of grant or rejection written | ||
A01 | Written decision to grant a patent or to grant a registration (utility model) |
Free format text: JAPANESE INTERMEDIATE CODE: A01 Effective date: 20100202 |
|
A01 | Written decision to grant a patent or to grant a registration (utility model) |
Free format text: JAPANESE INTERMEDIATE CODE: A01 |
|
A61 | First payment of annual fees (during grant procedure) |
Free format text: JAPANESE INTERMEDIATE CODE: A61 Effective date: 20100205 |
|
FPAY | Renewal fee payment (event date is renewal date of database) |
Free format text: PAYMENT UNTIL: 20130212 Year of fee payment: 3 |
|
R150 | Certificate of patent or registration of utility model |
Free format text: JAPANESE INTERMEDIATE CODE: R150 |
|
FPAY | Renewal fee payment (event date is renewal date of database) |
Free format text: PAYMENT UNTIL: 20140212 Year of fee payment: 4 |
|
R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
EXPY | Cancellation because of completion of term |