RU2246318C2 - Конъюгаты peg-уриказы и их использование - Google Patents
Конъюгаты peg-уриказы и их использование Download PDFInfo
- Publication number
- RU2246318C2 RU2246318C2 RU2001103144/15A RU2001103144A RU2246318C2 RU 2246318 C2 RU2246318 C2 RU 2246318C2 RU 2001103144/15 A RU2001103144/15 A RU 2001103144/15A RU 2001103144 A RU2001103144 A RU 2001103144A RU 2246318 C2 RU2246318 C2 RU 2246318C2
- Authority
- RU
- Russia
- Prior art keywords
- uricase
- peg
- conjugate according
- conjugate
- kda
- Prior art date
Links
- 108010092464 Urate Oxidase Proteins 0.000 title claims abstract description 331
- 108090000790 Enzymes Proteins 0.000 claims abstract description 43
- 102000004190 Enzymes Human genes 0.000 claims abstract description 43
- 230000001751 uricolytic effect Effects 0.000 claims abstract description 22
- LEHOTFFKMJEONL-UHFFFAOYSA-N Uric Acid Chemical compound N1C(=O)NC(=O)C2=C1NC(=O)N2 LEHOTFFKMJEONL-UHFFFAOYSA-N 0.000 claims description 36
- TVWHNULVHGKJHS-UHFFFAOYSA-N Uric acid Natural products N1C(=O)NC(=O)C2NC(=O)NC21 TVWHNULVHGKJHS-UHFFFAOYSA-N 0.000 claims description 29
- 229940116269 uric acid Drugs 0.000 claims description 29
- 210000004185 liver Anatomy 0.000 claims description 24
- 241000235646 Cyberlindnera jadinii Species 0.000 claims description 22
- 230000002163 immunogen Effects 0.000 claims description 22
- 241001504519 Papio ursinus Species 0.000 claims description 19
- 235000015277 pork Nutrition 0.000 claims description 16
- 241000228197 Aspergillus flavus Species 0.000 claims description 11
- 235000010469 Glycine max Nutrition 0.000 claims description 10
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 claims description 9
- 210000003041 ligament Anatomy 0.000 claims description 9
- 239000008194 pharmaceutical composition Substances 0.000 claims description 8
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 claims description 8
- 230000002538 fungal effect Effects 0.000 claims description 7
- 230000000813 microbial effect Effects 0.000 claims description 6
- 239000000203 mixture Substances 0.000 claims description 6
- 241000186074 Arthrobacter globiformis Species 0.000 claims description 5
- 241000196324 Embryophyta Species 0.000 claims description 5
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 claims description 5
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 claims description 4
- 241000283690 Bos taurus Species 0.000 claims description 3
- 241000255601 Drosophila melanogaster Species 0.000 claims description 3
- 241000255313 Drosophila pseudoobscura Species 0.000 claims description 3
- 244000068988 Glycine max Species 0.000 claims description 3
- 241000282520 Papio Species 0.000 claims description 3
- 241001494479 Pecora Species 0.000 claims description 3
- 239000003937 drug carrier Substances 0.000 claims description 3
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 claims description 2
- 150000001408 amides Chemical class 0.000 claims description 2
- 239000012530 fluid Substances 0.000 claims description 2
- 238000004108 freeze drying Methods 0.000 claims description 2
- 125000000467 secondary amino group Chemical class [H]N([*:1])[*:2] 0.000 claims description 2
- JOYRKODLDBILNP-UHFFFAOYSA-N Ethyl urethane Chemical compound CCOC(N)=O JOYRKODLDBILNP-UHFFFAOYSA-N 0.000 claims 1
- 238000007911 parenteral administration Methods 0.000 claims 1
- 229920001223 polyethylene glycol Polymers 0.000 abstract description 192
- 230000000694 effects Effects 0.000 abstract description 52
- 229940088598 enzyme Drugs 0.000 abstract description 40
- 238000000034 method Methods 0.000 abstract description 21
- 108010068701 Pegloticase Proteins 0.000 abstract description 8
- 239000000126 substance Substances 0.000 abstract description 4
- 229920003171 Poly (ethylene oxide) Polymers 0.000 abstract description 2
- 229940005267 urate oxidase Drugs 0.000 abstract 1
- 241000699670 Mus sp. Species 0.000 description 31
- 238000005303 weighing Methods 0.000 description 28
- 239000007924 injection Substances 0.000 description 26
- 238000002347 injection Methods 0.000 description 26
- 230000005847 immunogenicity Effects 0.000 description 24
- 238000009739 binding Methods 0.000 description 22
- 238000002360 preparation method Methods 0.000 description 20
- 230000002950 deficient Effects 0.000 description 18
- 230000002829 reductive effect Effects 0.000 description 18
- 230000006870 function Effects 0.000 description 15
- 210000002700 urine Anatomy 0.000 description 15
- 230000021615 conjugation Effects 0.000 description 14
- 235000018102 proteins Nutrition 0.000 description 14
- 108090000623 proteins and genes Proteins 0.000 description 14
- 102000004169 proteins and genes Human genes 0.000 description 14
- 238000011282 treatment Methods 0.000 description 14
- 239000000872 buffer Substances 0.000 description 13
- 201000001431 Hyperuricemia Diseases 0.000 description 12
- 210000002966 serum Anatomy 0.000 description 12
- 239000000243 solution Substances 0.000 description 12
- JYEUMXHLPRZUAT-UHFFFAOYSA-N 1,2,3-triazine Chemical compound C1=CN=NN=C1 JYEUMXHLPRZUAT-UHFFFAOYSA-N 0.000 description 11
- 235000001014 amino acid Nutrition 0.000 description 11
- 150000001413 amino acids Chemical class 0.000 description 10
- 125000003588 lysine group Chemical group [H]N([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 10
- 230000006320 pegylation Effects 0.000 description 10
- 238000012360 testing method Methods 0.000 description 10
- 229920000642 polymer Polymers 0.000 description 9
- 230000000717 retained effect Effects 0.000 description 9
- CDBYLPFSWZWCQE-UHFFFAOYSA-L Sodium Carbonate Chemical compound [Na+].[Na+].[O-]C([O-])=O CDBYLPFSWZWCQE-UHFFFAOYSA-L 0.000 description 8
- 230000007423 decrease Effects 0.000 description 8
- 229940079593 drug Drugs 0.000 description 8
- 239000003814 drug Substances 0.000 description 8
- 235000018977 lysine Nutrition 0.000 description 8
- 238000000746 purification Methods 0.000 description 8
- 241000699666 Mus <mouse, genus> Species 0.000 description 7
- 230000015572 biosynthetic process Effects 0.000 description 7
- 239000003795 chemical substances by application Substances 0.000 description 7
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 7
- 241001415846 Procellariidae Species 0.000 description 6
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 6
- 239000000427 antigen Substances 0.000 description 6
- 102000036639 antigens Human genes 0.000 description 6
- 108091007433 antigens Proteins 0.000 description 6
- 230000003247 decreasing effect Effects 0.000 description 6
- 238000005516 engineering process Methods 0.000 description 6
- 238000000386 microscopy Methods 0.000 description 6
- 238000003786 synthesis reaction Methods 0.000 description 6
- 201000005569 Gout Diseases 0.000 description 5
- 241000283973 Oryctolagus cuniculus Species 0.000 description 5
- 208000001647 Renal Insufficiency Diseases 0.000 description 5
- 125000003275 alpha amino acid group Chemical group 0.000 description 5
- 125000003277 amino group Chemical group 0.000 description 5
- 210000001124 body fluid Anatomy 0.000 description 5
- 239000010839 body fluid Substances 0.000 description 5
- 230000004087 circulation Effects 0.000 description 5
- 239000007928 intraperitoneal injection Substances 0.000 description 5
- 201000006370 kidney failure Diseases 0.000 description 5
- 239000002502 liposome Substances 0.000 description 5
- 230000014759 maintenance of location Effects 0.000 description 5
- 239000002904 solvent Substances 0.000 description 5
- 210000001519 tissue Anatomy 0.000 description 5
- LOVPHSMOAVXQIH-UHFFFAOYSA-N (4-nitrophenyl) hydrogen carbonate Chemical compound OC(=O)OC1=CC=C([N+]([O-])=O)C=C1 LOVPHSMOAVXQIH-UHFFFAOYSA-N 0.000 description 4
- 241000588724 Escherichia coli Species 0.000 description 4
- 241000124008 Mammalia Species 0.000 description 4
- 238000010521 absorption reaction Methods 0.000 description 4
- POJWUDADGALRAB-UHFFFAOYSA-N allantoin Chemical compound NC(=O)NC1NC(=O)NC1=O POJWUDADGALRAB-UHFFFAOYSA-N 0.000 description 4
- 210000004369 blood Anatomy 0.000 description 4
- 239000008280 blood Substances 0.000 description 4
- 238000006243 chemical reaction Methods 0.000 description 4
- 230000007547 defect Effects 0.000 description 4
- 230000008030 elimination Effects 0.000 description 4
- 238000003379 elimination reaction Methods 0.000 description 4
- 238000005342 ion exchange Methods 0.000 description 4
- 238000004255 ion exchange chromatography Methods 0.000 description 4
- 210000003734 kidney Anatomy 0.000 description 4
- 230000004048 modification Effects 0.000 description 4
- 238000012986 modification Methods 0.000 description 4
- 238000001542 size-exclusion chromatography Methods 0.000 description 4
- 229910000029 sodium carbonate Inorganic materials 0.000 description 4
- 238000010561 standard procedure Methods 0.000 description 4
- ZJIFDEVVTPEXDL-UHFFFAOYSA-N (2,5-dioxopyrrolidin-1-yl) hydrogen carbonate Chemical compound OC(=O)ON1C(=O)CCC1=O ZJIFDEVVTPEXDL-UHFFFAOYSA-N 0.000 description 3
- 238000002965 ELISA Methods 0.000 description 3
- IAYPIBMASNFSPL-UHFFFAOYSA-N Ethylene oxide Chemical class C1CO1 IAYPIBMASNFSPL-UHFFFAOYSA-N 0.000 description 3
- 241000282412 Homo Species 0.000 description 3
- 239000004472 Lysine Substances 0.000 description 3
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 3
- 201000005118 Nephrogenic diabetes insipidus Diseases 0.000 description 3
- 241000282887 Suidae Species 0.000 description 3
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 3
- 239000004473 Threonine Substances 0.000 description 3
- 238000010171 animal model Methods 0.000 description 3
- 230000000890 antigenic effect Effects 0.000 description 3
- 230000006378 damage Effects 0.000 description 3
- 201000010099 disease Diseases 0.000 description 3
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 3
- 230000002255 enzymatic effect Effects 0.000 description 3
- 230000002068 genetic effect Effects 0.000 description 3
- 230000000977 initiatory effect Effects 0.000 description 3
- 230000003211 malignant effect Effects 0.000 description 3
- 238000005259 measurement Methods 0.000 description 3
- 230000035772 mutation Effects 0.000 description 3
- 210000000056 organ Anatomy 0.000 description 3
- 230000002688 persistence Effects 0.000 description 3
- 238000004321 preservation Methods 0.000 description 3
- 239000000047 product Substances 0.000 description 3
- 238000000926 separation method Methods 0.000 description 3
- 239000011780 sodium chloride Substances 0.000 description 3
- 239000000758 substrate Substances 0.000 description 3
- 229920003169 water-soluble polymer Polymers 0.000 description 3
- NHBKXEKEPDILRR-UHFFFAOYSA-N 2,3-bis(butanoylsulfanyl)propyl butanoate Chemical compound CCCC(=O)OCC(SC(=O)CCC)CSC(=O)CCC NHBKXEKEPDILRR-UHFFFAOYSA-N 0.000 description 2
- POJWUDADGALRAB-PVQJCKRUSA-N Allantoin Natural products NC(=O)N[C@@H]1NC(=O)NC1=O POJWUDADGALRAB-PVQJCKRUSA-N 0.000 description 2
- 239000004475 Arginine Substances 0.000 description 2
- 241000186063 Arthrobacter Species 0.000 description 2
- 101000767281 Aspergillus flavus Uricase Proteins 0.000 description 2
- VEXZGXHMUGYJMC-UHFFFAOYSA-M Chloride anion Chemical compound [Cl-] VEXZGXHMUGYJMC-UHFFFAOYSA-M 0.000 description 2
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 2
- 206010025323 Lymphomas Diseases 0.000 description 2
- 101000608112 Mus musculus Uricase Proteins 0.000 description 2
- -1 N-hydroxysuccinimide carboxylic acid ester Chemical class 0.000 description 2
- 241000288906 Primates Species 0.000 description 2
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 2
- 239000012505 Superdex™ Substances 0.000 description 2
- 102000019197 Superoxide Dismutase Human genes 0.000 description 2
- 108010012715 Superoxide dismutase Proteins 0.000 description 2
- 101000608029 Sus scrofa Uricase Proteins 0.000 description 2
- 230000009471 action Effects 0.000 description 2
- 229960000458 allantoin Drugs 0.000 description 2
- 238000004458 analytical method Methods 0.000 description 2
- 238000012436 analytical size exclusion chromatography Methods 0.000 description 2
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 2
- 238000000149 argon plasma sintering Methods 0.000 description 2
- 230000008901 benefit Effects 0.000 description 2
- 210000004027 cell Anatomy 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 238000004587 chromatography analysis Methods 0.000 description 2
- 230000001684 chronic effect Effects 0.000 description 2
- 238000004140 cleaning Methods 0.000 description 2
- 238000004891 communication Methods 0.000 description 2
- 150000001875 compounds Chemical class 0.000 description 2
- 229940079919 digestives enzyme preparation Drugs 0.000 description 2
- 239000006185 dispersion Substances 0.000 description 2
- 230000007717 exclusion Effects 0.000 description 2
- 230000001900 immune effect Effects 0.000 description 2
- 230000008105 immune reaction Effects 0.000 description 2
- 238000000338 in vitro Methods 0.000 description 2
- 238000001727 in vivo Methods 0.000 description 2
- 239000003112 inhibitor Substances 0.000 description 2
- 208000017169 kidney disease Diseases 0.000 description 2
- 229920001427 mPEG Polymers 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 2
- 239000000546 pharmaceutical excipient Substances 0.000 description 2
- 230000002035 prolonged effect Effects 0.000 description 2
- 230000009145 protein modification Effects 0.000 description 2
- 238000011084 recovery Methods 0.000 description 2
- 238000003998 size exclusion chromatography high performance liquid chromatography Methods 0.000 description 2
- 239000003381 stabilizer Substances 0.000 description 2
- 238000002054 transplantation Methods 0.000 description 2
- 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 description 2
- 230000002485 urinary effect Effects 0.000 description 2
- NXLNNXIXOYSCMB-UHFFFAOYSA-N (4-nitrophenyl) carbonochloridate Chemical compound [O-][N+](=O)C1=CC=C(OC(Cl)=O)C=C1 NXLNNXIXOYSCMB-UHFFFAOYSA-N 0.000 description 1
- NWUYHJFMYQTDRP-UHFFFAOYSA-N 1,2-bis(ethenyl)benzene;1-ethenyl-2-ethylbenzene;styrene Chemical compound C=CC1=CC=CC=C1.CCC1=CC=CC=C1C=C.C=CC1=CC=CC=C1C=C NWUYHJFMYQTDRP-UHFFFAOYSA-N 0.000 description 1
- IXPNQXFRVYWDDI-UHFFFAOYSA-N 1-methyl-2,4-dioxo-1,3-diazinane-5-carboximidamide Chemical compound CN1CC(C(N)=N)C(=O)NC1=O IXPNQXFRVYWDDI-UHFFFAOYSA-N 0.000 description 1
- KVGVQTOQSNJTJI-UHFFFAOYSA-N 8-azaxanthine Chemical compound O=C1NC(=O)NC2=C1NN=N2 KVGVQTOQSNJTJI-UHFFFAOYSA-N 0.000 description 1
- 229920000936 Agarose Polymers 0.000 description 1
- 108010088751 Albumins Proteins 0.000 description 1
- 102000009027 Albumins Human genes 0.000 description 1
- 241000271566 Aves Species 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 208000019838 Blood disease Diseases 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 241000222120 Candida <Saccharomycetales> Species 0.000 description 1
- 241000700199 Cavia porcellus Species 0.000 description 1
- 229920001661 Chitosan Polymers 0.000 description 1
- 102000008186 Collagen Human genes 0.000 description 1
- 108010035532 Collagen Proteins 0.000 description 1
- 108020004635 Complementary DNA Proteins 0.000 description 1
- 206010010356 Congenital anomaly Diseases 0.000 description 1
- 102000004127 Cytokines Human genes 0.000 description 1
- 108090000695 Cytokines Proteins 0.000 description 1
- 230000004544 DNA amplification Effects 0.000 description 1
- 241001198387 Escherichia coli BL21(DE3) Species 0.000 description 1
- VGGSQFUCUMXWEO-UHFFFAOYSA-N Ethene Chemical compound C=C VGGSQFUCUMXWEO-UHFFFAOYSA-N 0.000 description 1
- 239000005977 Ethylene Substances 0.000 description 1
- 241000233866 Fungi Species 0.000 description 1
- 241000287828 Gallus gallus Species 0.000 description 1
- 229920002148 Gellan gum Polymers 0.000 description 1
- 101000767315 Glycine max Uricase-2 isozyme 1 Proteins 0.000 description 1
- 101000767285 Glycine max Uricase-2 isozyme 2 Proteins 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 206010020751 Hypersensitivity Diseases 0.000 description 1
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
- 240000006240 Linum usitatissimum Species 0.000 description 1
- 235000004431 Linum usitatissimum Nutrition 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 102000008300 Mutant Proteins Human genes 0.000 description 1
- 108010021466 Mutant Proteins Proteins 0.000 description 1
- 125000000729 N-terminal amino-acid group Chemical group 0.000 description 1
- 108090000854 Oxidoreductases Proteins 0.000 description 1
- 102000004316 Oxidoreductases Human genes 0.000 description 1
- 102000015731 Peptide Hormones Human genes 0.000 description 1
- 108010038988 Peptide Hormones Proteins 0.000 description 1
- 229920000954 Polyglycolide Polymers 0.000 description 1
- 239000012614 Q-Sepharose Substances 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 241000251539 Vertebrata <Metazoa> Species 0.000 description 1
- 230000001133 acceleration Effects 0.000 description 1
- 230000035508 accumulation Effects 0.000 description 1
- 238000009825 accumulation Methods 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 239000011149 active material Substances 0.000 description 1
- 239000000654 additive Substances 0.000 description 1
- 239000000443 aerosol Substances 0.000 description 1
- 150000001299 aldehydes Chemical class 0.000 description 1
- 239000003513 alkali Substances 0.000 description 1
- 239000012670 alkaline solution Substances 0.000 description 1
- OFCNXPDARWKPPY-UHFFFAOYSA-N allopurinol Chemical compound OC1=NC=NC2=C1C=NN2 OFCNXPDARWKPPY-UHFFFAOYSA-N 0.000 description 1
- 229960003459 allopurinol Drugs 0.000 description 1
- 150000001412 amines Chemical class 0.000 description 1
- 125000000539 amino acid group Chemical group 0.000 description 1
- 208000003455 anaphylaxis Diseases 0.000 description 1
- 210000001557 animal structure Anatomy 0.000 description 1
- 239000003963 antioxidant agent Substances 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 125000000637 arginyl group Chemical group N[C@@H](CCCNC(N)=N)C(=O)* 0.000 description 1
- 206010003246 arthritis Diseases 0.000 description 1
- 150000001540 azides Chemical class 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 230000017531 blood circulation Effects 0.000 description 1
- 229910021538 borax Inorganic materials 0.000 description 1
- 150000001642 boronic acid derivatives Chemical class 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- 239000007853 buffer solution Substances 0.000 description 1
- 244000309464 bull Species 0.000 description 1
- BPKIGYQJPYCAOW-FFJTTWKXSA-I calcium;potassium;disodium;(2s)-2-hydroxypropanoate;dichloride;dihydroxide;hydrate Chemical compound O.[OH-].[OH-].[Na+].[Na+].[Cl-].[Cl-].[K+].[Ca+2].C[C@H](O)C([O-])=O BPKIGYQJPYCAOW-FFJTTWKXSA-I 0.000 description 1
- 238000005251 capillar electrophoresis Methods 0.000 description 1
- 238000001818 capillary gel electrophoresis Methods 0.000 description 1
- OZMJXAQDMVDWBK-UHFFFAOYSA-N carbamic acid;ethyl carbamate Chemical compound NC(O)=O.CCOC(N)=O OZMJXAQDMVDWBK-UHFFFAOYSA-N 0.000 description 1
- 230000003197 catalytic effect Effects 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 238000007385 chemical modification Methods 0.000 description 1
- 239000007795 chemical reaction product Substances 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 235000013330 chicken meat Nutrition 0.000 description 1
- 229920001436 collagen Polymers 0.000 description 1
- 238000013270 controlled release Methods 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 238000012937 correction Methods 0.000 description 1
- MGNCLNQXLYJVJD-UHFFFAOYSA-N cyanuric chloride Chemical compound ClC1=NC(Cl)=NC(Cl)=N1 MGNCLNQXLYJVJD-UHFFFAOYSA-N 0.000 description 1
- 231100000433 cytotoxic Toxicity 0.000 description 1
- 230000001472 cytotoxic effect Effects 0.000 description 1
- 238000000354 decomposition reaction Methods 0.000 description 1
- 230000006735 deficit Effects 0.000 description 1
- 239000013578 denaturing buffer Substances 0.000 description 1
- 239000000539 dimer Substances 0.000 description 1
- 150000002009 diols Chemical class 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
- 238000012377 drug delivery Methods 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 238000010828 elution Methods 0.000 description 1
- 239000003995 emulsifying agent Substances 0.000 description 1
- 239000000839 emulsion Substances 0.000 description 1
- 238000005538 encapsulation Methods 0.000 description 1
- 239000013604 expression vector Substances 0.000 description 1
- 238000009472 formulation Methods 0.000 description 1
- 238000005194 fractionation Methods 0.000 description 1
- 230000005714 functional activity Effects 0.000 description 1
- 238000012817 gel-diffusion technique Methods 0.000 description 1
- 235000010492 gellan gum Nutrition 0.000 description 1
- 239000000216 gellan gum Substances 0.000 description 1
- 235000011187 glycerol Nutrition 0.000 description 1
- 238000001631 haemodialysis Methods 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 208000014951 hematologic disease Diseases 0.000 description 1
- 230000000322 hemodialysis Effects 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- 230000028993 immune response Effects 0.000 description 1
- 238000002513 implantation Methods 0.000 description 1
- 230000002779 inactivation Effects 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 238000001802 infusion Methods 0.000 description 1
- 238000007918 intramuscular administration Methods 0.000 description 1
- 239000007927 intramuscular injection Substances 0.000 description 1
- 238000007912 intraperitoneal administration Methods 0.000 description 1
- 238000001990 intravenous administration Methods 0.000 description 1
- 238000010253 intravenous injection Methods 0.000 description 1
- 239000003456 ion exchange resin Substances 0.000 description 1
- 229920003303 ion-exchange polymer Polymers 0.000 description 1
- 230000002147 killing effect Effects 0.000 description 1
- 238000011813 knockout mouse model Methods 0.000 description 1
- 208000032839 leukemia Diseases 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 125000005647 linker group Chemical group 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 238000004811 liquid chromatography Methods 0.000 description 1
- 238000012153 long-term therapy Methods 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 238000012423 maintenance Methods 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 239000000693 micelle Substances 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 108091005573 modified proteins Proteins 0.000 description 1
- 102000035118 modified proteins Human genes 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 210000000885 nephron Anatomy 0.000 description 1
- 231100000252 nontoxic Toxicity 0.000 description 1
- 230000003000 nontoxic effect Effects 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- 239000000813 peptide hormone Substances 0.000 description 1
- 230000008447 perception Effects 0.000 description 1
- 230000000858 peroxisomal effect Effects 0.000 description 1
- 210000002824 peroxisome Anatomy 0.000 description 1
- 230000003285 pharmacodynamic effect Effects 0.000 description 1
- 239000002953 phosphate buffered saline Substances 0.000 description 1
- 239000013612 plasmid Substances 0.000 description 1
- 229920000729 poly(L-lysine) polymer Polymers 0.000 description 1
- 229920000747 poly(lactic acid) Polymers 0.000 description 1
- 239000004633 polyglycolic acid Substances 0.000 description 1
- 239000004626 polylactic acid Substances 0.000 description 1
- 229920005862 polyol Polymers 0.000 description 1
- 150000003077 polyols Chemical class 0.000 description 1
- 229920001451 polypropylene glycol Polymers 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 238000004237 preparative chromatography Methods 0.000 description 1
- 239000003755 preservative agent Substances 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 102000004196 processed proteins & peptides Human genes 0.000 description 1
- 108090000765 processed proteins & peptides Proteins 0.000 description 1
- 150000003212 purines Chemical class 0.000 description 1
- 238000005215 recombination Methods 0.000 description 1
- 230000006798 recombination Effects 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 238000006722 reduction reaction Methods 0.000 description 1
- 238000005932 reductive alkylation reaction Methods 0.000 description 1
- 230000004044 response Effects 0.000 description 1
- 230000002441 reversible effect Effects 0.000 description 1
- 238000012552 review Methods 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 235000010413 sodium alginate Nutrition 0.000 description 1
- 239000000661 sodium alginate Substances 0.000 description 1
- 229940005550 sodium alginate Drugs 0.000 description 1
- BEOOHQFXGBMRKU-UHFFFAOYSA-N sodium cyanoborohydride Chemical compound [Na+].[B-]C#N BEOOHQFXGBMRKU-UHFFFAOYSA-N 0.000 description 1
- 235000010339 sodium tetraborate Nutrition 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 238000001179 sorption measurement Methods 0.000 description 1
- 210000000952 spleen Anatomy 0.000 description 1
- 238000007920 subcutaneous administration Methods 0.000 description 1
- 239000007929 subcutaneous injection Substances 0.000 description 1
- 238000006467 substitution reaction Methods 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 238000002560 therapeutic procedure Methods 0.000 description 1
- 150000003918 triazines Chemical class 0.000 description 1
- BSVBQGMMJUBVOD-UHFFFAOYSA-N trisodium borate Chemical compound [Na+].[Na+].[Na+].[O-]B([O-])[O-] BSVBQGMMJUBVOD-UHFFFAOYSA-N 0.000 description 1
- 238000000108 ultra-filtration Methods 0.000 description 1
- 239000000080 wetting agent Substances 0.000 description 1
Images
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
- C12N11/00—Carrier-bound or immobilised enzymes; Carrier-bound or immobilised microbial cells; Preparation thereof
- C12N11/02—Enzymes or microbial cells immobilised on or in an organic carrier
- C12N11/08—Enzymes or microbial cells immobilised on or in an organic carrier the carrier being a synthetic polymer
- C12N11/089—Enzymes or microbial cells immobilised on or in an organic carrier the carrier being a synthetic polymer obtained otherwise than by reactions only involving carbon-to-carbon unsaturated bonds
-
- 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
- C12N9/0004—Oxidoreductases (1.)
- C12N9/0012—Oxidoreductases (1.) acting on nitrogen containing compounds as donors (1.4, 1.5, 1.6, 1.7)
- C12N9/0044—Oxidoreductases (1.) acting on nitrogen containing compounds as donors (1.4, 1.5, 1.6, 1.7) acting on other nitrogen compounds as donors (1.7)
- C12N9/0046—Oxidoreductases (1.) acting on nitrogen containing compounds as donors (1.4, 1.5, 1.6, 1.7) acting on other nitrogen compounds as donors (1.7) with oxygen as acceptor (1.7.3)
-
- 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
- A61P13/00—Drugs for disorders of the urinary system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P13/00—Drugs for disorders of the urinary system
- A61P13/02—Drugs for disorders of the urinary system of urine or of the urinary tract, e.g. urine acidifiers
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P13/00—Drugs for disorders of the urinary system
- A61P13/12—Drugs for disorders of the urinary system of the kidneys
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P19/00—Drugs for skeletal disorders
- A61P19/06—Antigout agents, e.g. antihyperuricemic or uricosuric agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Medicinal Chemistry (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Genetics & Genomics (AREA)
- Urology & Nephrology (AREA)
- General Engineering & Computer Science (AREA)
- Biochemistry (AREA)
- Biotechnology (AREA)
- Epidemiology (AREA)
- Microbiology (AREA)
- Biomedical Technology (AREA)
- Molecular Biology (AREA)
- Immunology (AREA)
- Pain & Pain Management (AREA)
- Rheumatology (AREA)
- Physical Education & Sports Medicine (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Enzymes And Modification Thereof (AREA)
- Medicinal Preparation (AREA)
- Immobilizing And Processing Of Enzymes And Microorganisms (AREA)
- Investigating Or Analysing Biological Materials (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US13039298A | 1998-08-06 | 1998-08-06 | |
| US09/130,392 | 1998-08-06 |
Related Child Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| RU2004104953/15A Division RU2278680C2 (ru) | 1998-08-06 | 1999-08-02 | Способ изолирования тетрамерной формы уриказы и уриказа, полученная данным способом |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| RU2001103144A RU2001103144A (ru) | 2003-10-20 |
| RU2246318C2 true RU2246318C2 (ru) | 2005-02-20 |
Family
ID=22444494
Family Applications (3)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| RU2001103144/15A RU2246318C2 (ru) | 1998-08-06 | 1999-08-02 | Конъюгаты peg-уриказы и их использование |
| RU2004104953/15A RU2278680C2 (ru) | 1998-08-06 | 1999-08-02 | Способ изолирования тетрамерной формы уриказы и уриказа, полученная данным способом |
| RU2006107111/15A RU2349341C2 (ru) | 1998-08-06 | 2006-03-09 | Конъюгаты peg-уратоксидазы, их использование, способ изолирования тетрамерной формы уриказы |
Family Applications After (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| RU2004104953/15A RU2278680C2 (ru) | 1998-08-06 | 1999-08-02 | Способ изолирования тетрамерной формы уриказы и уриказа, полученная данным способом |
| RU2006107111/15A RU2349341C2 (ru) | 1998-08-06 | 2006-03-09 | Конъюгаты peg-уратоксидазы, их использование, способ изолирования тетрамерной формы уриказы |
Country Status (13)
| Country | Link |
|---|---|
| EP (1) | EP1100542B1 (enExample) |
| JP (3) | JP5183836B2 (enExample) |
| KR (2) | KR100614212B1 (enExample) |
| AU (1) | AU770014B2 (enExample) |
| BR (2) | BRPI9917760B8 (enExample) |
| CZ (1) | CZ303751B6 (enExample) |
| HU (2) | HU226294B1 (enExample) |
| IL (3) | IL141220A0 (enExample) |
| NZ (1) | NZ509595A (enExample) |
| PL (2) | PL202799B1 (enExample) |
| RU (3) | RU2246318C2 (enExample) |
| TW (1) | TW570981B (enExample) |
| WO (1) | WO2000007629A2 (enExample) |
Cited By (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| RU2382048C1 (ru) * | 2008-12-25 | 2010-02-20 | Общество С Ограниченной Ответственностью "Фармапарк" | Лекарственное средство на основе модифицированного интерферона альфа с пролонгированным терапевтическим действием |
| RU2604795C2 (ru) * | 2010-03-02 | 2016-12-10 | Проталикс Лтд. | Стабилизированная альфа-галактозидаза и ее применение |
| US11598767B2 (en) | 2009-06-25 | 2023-03-07 | Horizon Therapeutics Usa, Inc. | Methods and kits for predicting infusion reaction risk and antibody-mediated loss of response by monitoring serum uric acid during pegylated uricase therapy |
| US11781119B2 (en) | 2005-04-11 | 2023-10-10 | Horizon Therapeutics Usa, Inc. | Variant forms of urate oxidase and use thereof |
| RU2831122C2 (ru) * | 2019-06-04 | 2024-12-02 | Селекта Байосайенсиз, Инк. | Композиции и дозы пегилированной уриказы |
| US12194078B2 (en) | 2017-03-11 | 2025-01-14 | Cartesian Therapeutics, Inc. | Methods and compositions related to combined treatment with anti-inflammatories and synthetic nanocarriers comprising an immunosuppressant |
| US12465631B2 (en) | 2019-01-30 | 2025-11-11 | Horizon Therapeutics Usa, Inc. | Reducing immunogenicity to pegloticase |
| US12472167B2 (en) | 2013-05-03 | 2025-11-18 | Cartesian Therapeutics, Inc. | Methods providing a therapeutic macromolecule and synthetic nanocarriers comprising immunosuppressant locally and concomitantly to reduce both Type 1 and Type IV hypersensitivity |
Families Citing this family (32)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| PT1588716E (pt) | 1998-08-06 | 2011-05-25 | Mountain View Pharmaceuticals | Conjugados de peg-urato oxidase e sua utiliza??o |
| US6783965B1 (en) * | 2000-02-10 | 2004-08-31 | Mountain View Pharmaceuticals, Inc. | Aggregate-free urate oxidase for preparation of non-immunogenic polymer conjugates |
| AU766421B2 (en) | 1998-08-06 | 2003-10-16 | Duke University | Urate oxidase |
| IL141220A0 (en) * | 1998-08-06 | 2002-03-10 | Mountain View Pharmaceuticals | Conjugates of peg-urate oxidase and use thereof |
| AU2006203252B8 (en) * | 2000-02-10 | 2009-06-18 | Duke University | Aggregate-free urate oxidase for preparation of non-immunogenic polymer conjugates |
| US7455855B2 (en) | 2000-04-03 | 2008-11-25 | Santen Pharmaceutical Co., Ltd. | Delivering substance and drug delivery system using the same |
| US7799794B2 (en) | 2000-06-28 | 2010-09-21 | Merck Sharp & Dohme Corp. | Treatment for cardiovascular disease |
| DE60229958D1 (de) | 2001-06-28 | 2009-01-02 | Mountain View Pharmaceuticals | Polymerstabilisierte proteinasen |
| US6913915B2 (en) * | 2001-08-02 | 2005-07-05 | Phoenix Pharmacologics, Inc. | PEG-modified uricase |
| US8129330B2 (en) | 2002-09-30 | 2012-03-06 | Mountain View Pharmaceuticals, Inc. | Polymer conjugates with decreased antigenicity, methods of preparation and uses thereof |
| US20040062748A1 (en) | 2002-09-30 | 2004-04-01 | Mountain View Pharmaceuticals, Inc. | Polymer conjugates with decreased antigenicity, methods of preparation and uses thereof |
| MXPA05012314A (es) | 2003-05-12 | 2006-04-18 | Affymax Inc | Radical separador para peptido modificado con polietilenglicol. |
| PT1625156E (pt) | 2003-05-12 | 2013-01-09 | Affymax Inc | Novos péptidos que se fixam ao receptor da eritropoietina |
| KR101146160B1 (ko) * | 2004-06-30 | 2012-07-16 | 넥타르 테라퓨틱스 | 중합체인자 ｉｘ 부분의 접합체 |
| WO2006110761A2 (en) * | 2005-04-11 | 2006-10-19 | Savient Pharmaceuticals, Inc. | A variant form of urate oxidase and use thereof |
| US8148123B2 (en) | 2005-04-11 | 2012-04-03 | Savient Pharmaceuticals, Inc. | Methods for lowering elevated uric acid levels using intravenous injections of PEG-uricase |
| EP1883405A4 (en) | 2005-05-09 | 2010-01-27 | Takeda Pharmaceuticals North A | METHODS OF TREATING NEPHROLITHIASIS |
| US7550433B2 (en) | 2005-06-03 | 2009-06-23 | Affymax, Inc. | Erythropoietin receptor peptide formulations and uses |
| JP5033177B2 (ja) * | 2006-04-12 | 2012-09-26 | サビエント ファーマセウティカルズ インク． | 陽イオン界面活性剤によるタンパク質の精製 |
| JP4890132B2 (ja) * | 2006-07-20 | 2012-03-07 | 東洋紡績株式会社 | ウリカーゼの比活性を向上させる方法、および比活性の向上した改変型ウリカーゼ |
| CN103298466B (zh) | 2010-09-10 | 2015-11-25 | 武田制药美国有限公司 | 茶碱和非布索坦的联合治疗方法 |
| CN102634492B (zh) | 2011-02-14 | 2015-06-10 | 重庆富进生物医药有限公司 | 聚乙二醇化犬源尿酸氧化酶类似物及其制备方法和应用 |
| WO2013151638A1 (en) | 2012-04-06 | 2013-10-10 | Indus Pharmaceuticals, Inc. | Novel compositions of combinations of non-covalent dna binding agents and anti-cancer and/or anti-inflammatory agents and their use in disease treatment |
| MX2017014547A (es) * | 2015-05-15 | 2018-03-15 | Medimmune Llc | Secuencias de uricasa mejoradas y metodos de tratamiento. |
| CN105412942B (zh) * | 2015-12-23 | 2019-02-26 | 沈阳三生制药有限责任公司 | 聚乙二醇化的重组产朊假丝酵母尿酸氧化酶冻干注射剂 |
| CN112980808B (zh) * | 2019-12-12 | 2024-10-29 | 深圳迈瑞生物医疗电子股份有限公司 | 尿酸酶、及其制备方法和用途 |
| KR20230110281A (ko) | 2020-11-03 | 2023-07-21 | 프로탈릭스 리미티드 | 변형된 유리카제(uricase) 및 이의 용도 |
| CN114438047B (zh) * | 2020-11-05 | 2024-11-22 | 重庆派金生物科技有限公司 | 制备聚乙二醇修饰的尿酸氧化酶的方法 |
| CN114438048B (zh) * | 2020-11-05 | 2024-10-22 | 重庆派金生物科技有限公司 | 尿酸氧化酶制剂及其应用 |
| CA3211023A1 (en) | 2021-02-10 | 2022-08-18 | Oriental Yeast Co., Ltd. | Uricase activator and uric acid measurement reagent |
| CN114181917B (zh) * | 2022-02-14 | 2022-06-03 | 潍坊华卓生物科技有限公司 | 一种改造尿酸酶、基因序列、制备方法及应用 |
| US12269875B2 (en) | 2023-08-03 | 2025-04-08 | Jeff R. Peterson | Gout flare prevention methods using IL-1BETA blockers |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4179337A (en) * | 1973-07-20 | 1979-12-18 | Davis Frank F | Non-immunogenic polypeptides |
| RU2105812C1 (ru) * | 1989-07-13 | 1998-02-27 | Санофи | Полипептид, обладающий уратоксидазной активностью, фрагмент днк, обеспечивающий экспрессию полипептида с уратоксидазной активностью (варианты), вектор экспрессии, содержащий фрагмент днк, обеспечивающий экспрессию полипептида с уратоксидазной активностью (варианты), штамм, экспрессирующий полипептид, обладающий уратоксидазной активностью (варианты), способ получения полипептида, обладающего уратоксидазной активностью |
Family Cites Families (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| FR1529675A (fr) * | 1967-03-29 | 1968-06-21 | Applic Biochimiques Soc Et | Urate oxydase à haute activité et sa préparation |
| US3616231A (en) * | 1968-11-14 | 1971-10-26 | Boehringer Mannheim Gmbh | Process for the production of uricase |
| JPS6031472B2 (ja) * | 1978-12-14 | 1985-07-22 | 協和醗酵工業株式会社 | 酸性ウリカ−ゼ |
| JPS55135590A (en) * | 1979-04-05 | 1980-10-22 | Mihama Hisaharu | Modified asparaginase and uricase and their preparation |
| JPS57192435A (en) * | 1981-05-20 | 1982-11-26 | Toyobo Co Ltd | Modified polypeptide |
| JPS6255079A (ja) * | 1986-04-23 | 1987-03-10 | Mihama Hisaharu | 修飾ウリカ−ゼ |
| AU766421B2 (en) * | 1998-08-06 | 2003-10-16 | Duke University | Urate oxidase |
| US6783965B1 (en) * | 2000-02-10 | 2004-08-31 | Mountain View Pharmaceuticals, Inc. | Aggregate-free urate oxidase for preparation of non-immunogenic polymer conjugates |
| IL141220A0 (en) * | 1998-08-06 | 2002-03-10 | Mountain View Pharmaceuticals | Conjugates of peg-urate oxidase and use thereof |
-
1999
- 1999-08-02 IL IL14122099A patent/IL141220A0/xx active IP Right Grant
- 1999-08-02 NZ NZ509595A patent/NZ509595A/xx not_active IP Right Cessation
- 1999-08-02 BR BRPI9917760A patent/BRPI9917760B8/pt not_active IP Right Cessation
- 1999-08-02 WO PCT/US1999/017514 patent/WO2000007629A2/en not_active Ceased
- 1999-08-02 RU RU2001103144/15A patent/RU2246318C2/ru not_active IP Right Cessation
- 1999-08-02 KR KR1020047014428A patent/KR100614212B1/ko not_active Expired - Fee Related
- 1999-08-02 PL PL380583A patent/PL202799B1/pl unknown
- 1999-08-02 HU HU0103003A patent/HU226294B1/hu not_active IP Right Cessation
- 1999-08-02 RU RU2004104953/15A patent/RU2278680C2/ru not_active IP Right Cessation
- 1999-08-02 AU AU52515/99A patent/AU770014B2/en not_active Ceased
- 1999-08-02 CZ CZ20010317A patent/CZ303751B6/cs not_active IP Right Cessation
- 1999-08-02 BR BRPI9912974A patent/BRPI9912974B8/pt not_active IP Right Cessation
- 1999-08-02 EP EP99937745A patent/EP1100542B1/en not_active Expired - Lifetime
- 1999-08-02 PL PL383331A patent/PL220873B1/pl unknown
- 1999-08-02 JP JP2000563311A patent/JP5183836B2/ja not_active Expired - Fee Related
- 1999-08-02 HU HU0800112A patent/HU228916B1/hu not_active IP Right Cessation
- 1999-08-02 KR KR10-2001-7001569A patent/KR100488848B1/ko not_active Expired - Fee Related
- 1999-08-05 TW TW088113406A patent/TW570981B/zh not_active IP Right Cessation
-
2001
- 2001-02-01 IL IL141220A patent/IL141220A/en not_active IP Right Cessation
-
2006
- 2006-03-09 RU RU2006107111/15A patent/RU2349341C2/ru not_active IP Right Cessation
-
2007
- 2007-06-14 IL IL183948A patent/IL183948A/en not_active IP Right Cessation
-
2009
- 2009-07-24 JP JP2009173148A patent/JP5290901B2/ja not_active Expired - Fee Related
-
2012
- 2012-11-12 JP JP2012248770A patent/JP5291235B2/ja not_active Expired - Fee Related
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4179337A (en) * | 1973-07-20 | 1979-12-18 | Davis Frank F | Non-immunogenic polypeptides |
| RU2105812C1 (ru) * | 1989-07-13 | 1998-02-27 | Санофи | Полипептид, обладающий уратоксидазной активностью, фрагмент днк, обеспечивающий экспрессию полипептида с уратоксидазной активностью (варианты), вектор экспрессии, содержащий фрагмент днк, обеспечивающий экспрессию полипептида с уратоксидазной активностью (варианты), штамм, экспрессирующий полипептид, обладающий уратоксидазной активностью (варианты), способ получения полипептида, обладающего уратоксидазной активностью |
Cited By (12)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US11781119B2 (en) | 2005-04-11 | 2023-10-10 | Horizon Therapeutics Usa, Inc. | Variant forms of urate oxidase and use thereof |
| RU2382048C1 (ru) * | 2008-12-25 | 2010-02-20 | Общество С Ограниченной Ответственностью "Фармапарк" | Лекарственное средство на основе модифицированного интерферона альфа с пролонгированным терапевтическим действием |
| US11598767B2 (en) | 2009-06-25 | 2023-03-07 | Horizon Therapeutics Usa, Inc. | Methods and kits for predicting infusion reaction risk and antibody-mediated loss of response by monitoring serum uric acid during pegylated uricase therapy |
| US11639927B2 (en) | 2009-06-25 | 2023-05-02 | Horizon Therapeutics Usa, Inc. | Methods and kits for predicting infusion reaction risk and antibody-mediated loss of response by monitoring serum uric acid during PEGylated uricase therapy |
| US11982670B2 (en) | 2009-06-25 | 2024-05-14 | Horizon Therapeutics Usa, Inc. | Methods and kits for predicting infusion reaction risk and antibody-mediated loss of response by monitoring serum uric acid during pegylated uricase therapy |
| US12188927B2 (en) | 2009-06-25 | 2025-01-07 | Horizon Therapeutics Usa, Inc. | Methods and kits for predicting infusion reaction risk and antibody-mediated loss of response by monitoring serum uric acid during PEGylated uricase therapy |
| RU2604795C2 (ru) * | 2010-03-02 | 2016-12-10 | Проталикс Лтд. | Стабилизированная альфа-галактозидаза и ее применение |
| US12472167B2 (en) | 2013-05-03 | 2025-11-18 | Cartesian Therapeutics, Inc. | Methods providing a therapeutic macromolecule and synthetic nanocarriers comprising immunosuppressant locally and concomitantly to reduce both Type 1 and Type IV hypersensitivity |
| US12194078B2 (en) | 2017-03-11 | 2025-01-14 | Cartesian Therapeutics, Inc. | Methods and compositions related to combined treatment with anti-inflammatories and synthetic nanocarriers comprising an immunosuppressant |
| US12496331B2 (en) | 2017-11-10 | 2025-12-16 | Horizon Therapeutics Usa, Inc. | Combination therapies of prednisone and uricase molecules and uses thereof |
| US12465631B2 (en) | 2019-01-30 | 2025-11-11 | Horizon Therapeutics Usa, Inc. | Reducing immunogenicity to pegloticase |
| RU2831122C2 (ru) * | 2019-06-04 | 2024-12-02 | Селекта Байосайенсиз, Инк. | Композиции и дозы пегилированной уриказы |
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| RU2246318C2 (ru) | Конъюгаты peg-уриказы и их использование | |
| US9885024B2 (en) | PEG-urate oxidase conjugates and use thereof | |
| RU2443426C2 (ru) | Конъюгаты уратоксидазы, фармацевтическая композиция для снижения уровней мочевой кислоты и способ получения вышеупомянутых конъюгатов | |
| HK1155080A (en) | Isolated tetrameric uricase | |
| HK1155080B (en) | Isolated tetrameric uricase | |
| HK1037330B (en) | Peg-urate oxidase conjugates and use thereof | |
| HK1141738B (en) | Peg-urate oxidase conjugates and use thereof | |
| MXPA01001272A (en) | Peg-urate oxidase conjugates and use thereof |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| MM4A | The patent is invalid due to non-payment of fees |
Effective date: 20180803 |