CA2951766A1 - Process for the purification of tnfr:fc fusion protein - Google Patents
Process for the purification of tnfr:fc fusion protein Download PDFInfo
- Publication number
- CA2951766A1 CA2951766A1 CA2951766A CA2951766A CA2951766A1 CA 2951766 A1 CA2951766 A1 CA 2951766A1 CA 2951766 A CA2951766 A CA 2951766A CA 2951766 A CA2951766 A CA 2951766A CA 2951766 A1 CA2951766 A1 CA 2951766A1
- Authority
- CA
- Canada
- Prior art keywords
- protein
- tnfr
- chromatography column
- fusion protein
- hcp
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Abandoned
Links
- 108091006020 Fc-tagged proteins Proteins 0.000 title claims abstract description 127
- 238000000034 method Methods 0.000 title claims abstract description 99
- 230000008569 process Effects 0.000 title claims abstract description 94
- 238000000746 purification Methods 0.000 title claims abstract description 36
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 309
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 309
- 108060008683 Tumor Necrosis Factor Receptor Proteins 0.000 claims abstract description 138
- 102000003298 tumor necrosis factor receptor Human genes 0.000 claims abstract description 138
- 238000012434 mixed-mode chromatography Methods 0.000 claims abstract description 72
- 102000004190 Enzymes Human genes 0.000 claims abstract description 58
- 108090000790 Enzymes Proteins 0.000 claims abstract description 58
- 230000000593 degrading effect Effects 0.000 claims abstract description 56
- 238000001042 affinity chromatography Methods 0.000 claims abstract description 48
- 239000000203 mixture Substances 0.000 claims description 141
- 239000012535 impurity Substances 0.000 claims description 85
- 238000004191 hydrophobic interaction chromatography Methods 0.000 claims description 57
- 239000000872 buffer Substances 0.000 claims description 54
- 238000005571 anion exchange chromatography Methods 0.000 claims description 29
- 239000006167 equilibration buffer Substances 0.000 claims description 29
- 238000004587 chromatography analysis Methods 0.000 claims description 24
- 108010008165 Etanercept Proteins 0.000 claims description 23
- 108091005804 Peptidases Proteins 0.000 claims description 23
- 239000004365 Protease Substances 0.000 claims description 23
- 229960000403 etanercept Drugs 0.000 claims description 23
- 239000011534 wash buffer Substances 0.000 claims description 23
- 102000035195 Peptidases Human genes 0.000 claims description 21
- 239000003446 ligand Substances 0.000 claims description 17
- 239000012149 elution buffer Substances 0.000 claims description 15
- 230000003993 interaction Effects 0.000 claims description 13
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 claims description 12
- 239000001632 sodium acetate Substances 0.000 claims description 12
- 235000017281 sodium acetate Nutrition 0.000 claims description 12
- QZNNVYOVQUKYSC-JEDNCBNOSA-N (2s)-2-amino-3-(1h-imidazol-5-yl)propanoic acid;hydron;chloride Chemical compound Cl.OC(=O)[C@@H](N)CC1=CN=CN1 QZNNVYOVQUKYSC-JEDNCBNOSA-N 0.000 claims description 11
- 239000007983 Tris buffer Substances 0.000 claims description 11
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 claims description 11
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 claims description 10
- 239000011347 resin Substances 0.000 claims description 10
- 229920005989 resin Polymers 0.000 claims description 10
- JUJWROOIHBZHMG-UHFFFAOYSA-N Pyridine Chemical compound C1=CC=NC=C1 JUJWROOIHBZHMG-UHFFFAOYSA-N 0.000 claims description 8
- 238000010828 elution Methods 0.000 claims description 8
- 230000004927 fusion Effects 0.000 claims description 6
- 238000005406 washing Methods 0.000 claims description 6
- WOUANPHGFPAJCA-UHFFFAOYSA-N 2-[benzyl(methyl)amino]ethanol Chemical compound OCCN(C)CC1=CC=CC=C1 WOUANPHGFPAJCA-UHFFFAOYSA-N 0.000 claims description 5
- 239000012634 fragment Substances 0.000 claims description 5
- 239000011780 sodium chloride Substances 0.000 claims description 5
- LYUQWQRTDLVQGA-UHFFFAOYSA-N 3-phenylpropylamine Chemical compound NCCCC1=CC=CC=C1 LYUQWQRTDLVQGA-UHFFFAOYSA-N 0.000 claims description 4
- KRKNYBCHXYNGOX-UHFFFAOYSA-K Citrate Chemical compound [O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O KRKNYBCHXYNGOX-UHFFFAOYSA-K 0.000 claims description 4
- 125000000484 butyl group Chemical group [H]C([*])([H])C([H])([H])C([H])([H])C([H])([H])[H] 0.000 claims description 4
- 239000013019 capto adhere Substances 0.000 claims description 4
- UMJSCPRVCHMLSP-UHFFFAOYSA-N pyridine Natural products COC1=CC=CN=C1 UMJSCPRVCHMLSP-UHFFFAOYSA-N 0.000 claims description 4
- BMVXCPBXGZKUPN-UHFFFAOYSA-N 1-hexanamine Chemical compound CCCCCCN BMVXCPBXGZKUPN-UHFFFAOYSA-N 0.000 claims description 3
- JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-UHFFFAOYSA-N 0.000 claims description 3
- 239000007995 HEPES buffer Substances 0.000 claims description 3
- 229910019142 PO4 Inorganic materials 0.000 claims description 3
- 229920002684 Sepharose Polymers 0.000 claims description 3
- 239000002158 endotoxin Substances 0.000 claims description 3
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 claims description 3
- 239000010452 phosphate Substances 0.000 claims description 3
- CIJQGPVMMRXSQW-UHFFFAOYSA-M sodium;2-aminoacetic acid;hydroxide Chemical compound O.[Na+].NCC([O-])=O CIJQGPVMMRXSQW-UHFFFAOYSA-M 0.000 claims description 3
- 239000012619 Butyl Sepharose® Substances 0.000 claims description 2
- 101710120037 Toxin CcdB Proteins 0.000 claims description 2
- GSEJCLTVZPLZKY-UHFFFAOYSA-N Triethanolamine Chemical compound OCCN(CCO)CCO GSEJCLTVZPLZKY-UHFFFAOYSA-N 0.000 claims description 2
- 241000700605 Viruses Species 0.000 claims description 2
- 108020004707 nucleic acids Proteins 0.000 claims description 2
- 102000039446 nucleic acids Human genes 0.000 claims description 2
- 150000007523 nucleic acids Chemical class 0.000 claims description 2
- 125000001997 phenyl group Chemical group [H]C1=C([H])C([H])=C(*)C([H])=C1[H] 0.000 claims description 2
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims 2
- MZVQCMJNVPIDEA-UHFFFAOYSA-N [CH2]CN(CC)CC Chemical group [CH2]CN(CC)CC MZVQCMJNVPIDEA-UHFFFAOYSA-N 0.000 claims 2
- 238000011067 equilibration Methods 0.000 claims 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 claims 1
- QGZKDVFQNNGYKY-UHFFFAOYSA-O Ammonium Chemical compound [NH4+] QGZKDVFQNNGYKY-UHFFFAOYSA-O 0.000 claims 1
- LSNNMFCWUKXFEE-UHFFFAOYSA-M Bisulfite Chemical compound OS([O-])=O LSNNMFCWUKXFEE-UHFFFAOYSA-M 0.000 claims 1
- 125000002057 carboxymethyl group Chemical group [H]OC(=O)C([H])([H])[*] 0.000 claims 1
- 239000012561 harvest cell culture fluid Substances 0.000 description 21
- 210000004027 cell Anatomy 0.000 description 19
- 230000015556 catabolic process Effects 0.000 description 16
- 238000006731 degradation reaction Methods 0.000 description 16
- 238000011068 loading method Methods 0.000 description 13
- 230000000694 effects Effects 0.000 description 12
- 238000004128 high performance liquid chromatography Methods 0.000 description 12
- 239000003550 marker Substances 0.000 description 12
- 238000005349 anion exchange Methods 0.000 description 10
- 230000002209 hydrophobic effect Effects 0.000 description 10
- BNIILDVGGAEEIG-UHFFFAOYSA-L disodium hydrogen phosphate Chemical compound [Na+].[Na+].OP([O-])([O-])=O BNIILDVGGAEEIG-UHFFFAOYSA-L 0.000 description 9
- NLJMYIDDQXHKNR-UHFFFAOYSA-K sodium citrate Chemical compound O.O.[Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O NLJMYIDDQXHKNR-UHFFFAOYSA-K 0.000 description 9
- 241000894007 species Species 0.000 description 9
- 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 8
- 102000013382 Gelatinases Human genes 0.000 description 8
- 108010026132 Gelatinases Proteins 0.000 description 8
- KFZMGEQAYNKOFK-UHFFFAOYSA-N Isopropanol Chemical compound CC(C)O KFZMGEQAYNKOFK-UHFFFAOYSA-N 0.000 description 8
- 238000007804 gelatin zymography Methods 0.000 description 8
- 239000012145 high-salt buffer Substances 0.000 description 8
- 108091006629 SLC13A2 Proteins 0.000 description 7
- 230000027455 binding Effects 0.000 description 7
- 238000011026 diafiltration Methods 0.000 description 7
- 238000002965 ELISA Methods 0.000 description 6
- 108010010803 Gelatin Proteins 0.000 description 6
- 238000004458 analytical method Methods 0.000 description 6
- 239000008273 gelatin Substances 0.000 description 6
- 229920000159 gelatin Polymers 0.000 description 6
- 235000019322 gelatine Nutrition 0.000 description 6
- 235000011852 gelatine desserts Nutrition 0.000 description 6
- 238000004255 ion exchange chromatography Methods 0.000 description 6
- 239000000047 product Substances 0.000 description 6
- 230000003612 virological effect Effects 0.000 description 6
- 102000018594 Tumour necrosis factor Human genes 0.000 description 5
- 108050007852 Tumour necrosis factor Proteins 0.000 description 5
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 5
- 239000004202 carbamide Substances 0.000 description 5
- 238000004113 cell culture Methods 0.000 description 5
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 5
- 238000011210 chromatographic step Methods 0.000 description 5
- 238000004440 column chromatography Methods 0.000 description 5
- 238000001514 detection method Methods 0.000 description 5
- 238000011534 incubation Methods 0.000 description 5
- 239000012460 protein solution Substances 0.000 description 5
- 239000012515 MabSelect SuRe Substances 0.000 description 4
- 238000005277 cation exchange chromatography Methods 0.000 description 4
- 239000000356 contaminant Substances 0.000 description 4
- 230000002779 inactivation Effects 0.000 description 4
- 239000011159 matrix material Substances 0.000 description 4
- 235000010482 polyoxyethylene sorbitan monooleate Nutrition 0.000 description 4
- 229920001184 polypeptide Polymers 0.000 description 4
- 229920000053 polysorbate 80 Polymers 0.000 description 4
- 238000011176 pooling Methods 0.000 description 4
- 102000004196 processed proteins & peptides Human genes 0.000 description 4
- 108090000765 processed proteins & peptides Proteins 0.000 description 4
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 4
- 239000008215 water for injection Substances 0.000 description 4
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 3
- 241000699802 Cricetulus griseus Species 0.000 description 3
- 102000004127 Cytokines Human genes 0.000 description 3
- 108090000695 Cytokines Proteins 0.000 description 3
- 229920002271 DEAE-Sepharose Polymers 0.000 description 3
- 102000005741 Metalloproteases Human genes 0.000 description 3
- 108010006035 Metalloproteases Proteins 0.000 description 3
- 238000002835 absorbance Methods 0.000 description 3
- 239000000654 additive Substances 0.000 description 3
- -1 belatacept Proteins 0.000 description 3
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 description 3
- 238000009295 crossflow filtration Methods 0.000 description 3
- 230000007423 decrease Effects 0.000 description 3
- 238000005516 engineering process Methods 0.000 description 3
- 230000007717 exclusion Effects 0.000 description 3
- 108020001507 fusion proteins Proteins 0.000 description 3
- 102000037865 fusion proteins Human genes 0.000 description 3
- RAXXELZNTBOGNW-UHFFFAOYSA-N imidazole Natural products C1=CNC=N1 RAXXELZNTBOGNW-UHFFFAOYSA-N 0.000 description 3
- 239000012528 membrane Substances 0.000 description 3
- 239000000178 monomer Substances 0.000 description 3
- 239000002245 particle Substances 0.000 description 3
- 239000012562 protein A resin Substances 0.000 description 3
- 102000005962 receptors Human genes 0.000 description 3
- 108020003175 receptors Proteins 0.000 description 3
- 230000035945 sensitivity Effects 0.000 description 3
- 238000000926 separation method Methods 0.000 description 3
- 239000001509 sodium citrate Substances 0.000 description 3
- 239000000243 solution Substances 0.000 description 3
- 239000000758 substrate Substances 0.000 description 3
- HRXKRNGNAMMEHJ-UHFFFAOYSA-K trisodium citrate Chemical compound [Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O HRXKRNGNAMMEHJ-UHFFFAOYSA-K 0.000 description 3
- 229940038773 trisodium citrate Drugs 0.000 description 3
- LRZSAGKIMYFLHY-UHFFFAOYSA-N 2-hydroxypropane-1,2,3-tricarboxylic acid;dihydrate Chemical compound O.O.OC(=O)CC(O)(C(O)=O)CC(O)=O LRZSAGKIMYFLHY-UHFFFAOYSA-N 0.000 description 2
- BTBUEUYNUDRHOZ-UHFFFAOYSA-N Borate Chemical compound [O-]B([O-])[O-] BTBUEUYNUDRHOZ-UHFFFAOYSA-N 0.000 description 2
- VEXZGXHMUGYJMC-UHFFFAOYSA-M Chloride anion Chemical compound [Cl-] VEXZGXHMUGYJMC-UHFFFAOYSA-M 0.000 description 2
- 108020004511 Recombinant DNA Proteins 0.000 description 2
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 2
- 108060008682 Tumor Necrosis Factor Proteins 0.000 description 2
- 239000002253 acid Substances 0.000 description 2
- 150000007513 acids Chemical class 0.000 description 2
- 150000001450 anions Chemical class 0.000 description 2
- 239000012539 chromatography resin Substances 0.000 description 2
- 238000005352 clarification Methods 0.000 description 2
- 230000001143 conditioned effect Effects 0.000 description 2
- 230000003247 decreasing effect Effects 0.000 description 2
- 230000029087 digestion Effects 0.000 description 2
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 2
- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 2
- 239000000499 gel Substances 0.000 description 2
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 2
- 239000001257 hydrogen Substances 0.000 description 2
- 229910052739 hydrogen Inorganic materials 0.000 description 2
- 230000005764 inhibitory process Effects 0.000 description 2
- NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 description 2
- 230000007774 longterm Effects 0.000 description 2
- 210000004962 mammalian cell Anatomy 0.000 description 2
- WWZKQHOCKIZLMA-UHFFFAOYSA-N octanoic acid Chemical compound CCCCCCCC(O)=O WWZKQHOCKIZLMA-UHFFFAOYSA-N 0.000 description 2
- 210000001672 ovary Anatomy 0.000 description 2
- 238000005498 polishing Methods 0.000 description 2
- 238000002360 preparation method Methods 0.000 description 2
- 230000002797 proteolythic effect Effects 0.000 description 2
- 230000009467 reduction Effects 0.000 description 2
- 239000012465 retentate Substances 0.000 description 2
- 206010039073 rheumatoid arthritis Diseases 0.000 description 2
- 238000003998 size exclusion chromatography high performance liquid chromatography Methods 0.000 description 2
- 239000011550 stock solution Substances 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 238000011100 viral filtration Methods 0.000 description 2
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 2
- MZOFCQQQCNRIBI-VMXHOPILSA-N (3s)-4-[[(2s)-1-[[(2s)-1-[[(1s)-1-carboxy-2-hydroxyethyl]amino]-4-methyl-1-oxopentan-2-yl]amino]-5-(diaminomethylideneamino)-1-oxopentan-2-yl]amino]-3-[[2-[[(2s)-2,6-diaminohexanoyl]amino]acetyl]amino]-4-oxobutanoic acid Chemical compound OC[C@@H](C(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H](CC(O)=O)NC(=O)CNC(=O)[C@@H](N)CCCCN MZOFCQQQCNRIBI-VMXHOPILSA-N 0.000 description 1
- BFSVOASYOCHEOV-UHFFFAOYSA-N 2-diethylaminoethanol Chemical compound CCN(CC)CCO BFSVOASYOCHEOV-UHFFFAOYSA-N 0.000 description 1
- QTBSBXVTEAMEQO-UHFFFAOYSA-M Acetate Chemical compound CC([O-])=O QTBSBXVTEAMEQO-UHFFFAOYSA-M 0.000 description 1
- 239000005635 Caprylic acid (CAS 124-07-2) Substances 0.000 description 1
- 102000000844 Cell Surface Receptors Human genes 0.000 description 1
- 108010001857 Cell Surface Receptors Proteins 0.000 description 1
- 208000011231 Crohn disease Diseases 0.000 description 1
- 201000003883 Cystic fibrosis Diseases 0.000 description 1
- 108020004414 DNA Proteins 0.000 description 1
- 102000003951 Erythropoietin Human genes 0.000 description 1
- 108090000394 Erythropoietin Proteins 0.000 description 1
- 101150089023 FASLG gene Proteins 0.000 description 1
- 102000003886 Glycoproteins Human genes 0.000 description 1
- 108090000288 Glycoproteins Proteins 0.000 description 1
- 238000012855 HCP-ELISA Methods 0.000 description 1
- 208000031220 Hemophilia Diseases 0.000 description 1
- 208000009292 Hemophilia A Diseases 0.000 description 1
- 206010061218 Inflammation Diseases 0.000 description 1
- 102000004877 Insulin Human genes 0.000 description 1
- 108090001061 Insulin Proteins 0.000 description 1
- 102000014150 Interferons Human genes 0.000 description 1
- 108010050904 Interferons Proteins 0.000 description 1
- 206010028980 Neoplasm Diseases 0.000 description 1
- 201000001263 Psoriatic Arthritis Diseases 0.000 description 1
- 208000036824 Psoriatic arthropathy Diseases 0.000 description 1
- 208000006011 Stroke Diseases 0.000 description 1
- 229920004890 Triton X-100 Polymers 0.000 description 1
- 239000013504 Triton X-100 Substances 0.000 description 1
- 102000000852 Tumor Necrosis Factor-alpha Human genes 0.000 description 1
- 102100031988 Tumor necrosis factor ligand superfamily member 6 Human genes 0.000 description 1
- 229960003697 abatacept Drugs 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 239000008186 active pharmaceutical agent Substances 0.000 description 1
- 229960002964 adalimumab Drugs 0.000 description 1
- 108010081667 aflibercept Proteins 0.000 description 1
- 229960002833 aflibercept Drugs 0.000 description 1
- 238000005054 agglomeration Methods 0.000 description 1
- 239000012615 aggregate Substances 0.000 description 1
- 230000002776 aggregation Effects 0.000 description 1
- 229960002459 alefacept Drugs 0.000 description 1
- 150000001412 amines Chemical class 0.000 description 1
- 150000001413 amino acids Chemical class 0.000 description 1
- 208000007502 anemia Diseases 0.000 description 1
- 239000000427 antigen Substances 0.000 description 1
- 108091007433 antigens Proteins 0.000 description 1
- 102000036639 antigens Human genes 0.000 description 1
- 238000010923 batch production Methods 0.000 description 1
- 229960005347 belatacept Drugs 0.000 description 1
- 239000003124 biologic agent Substances 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 230000008512 biological response Effects 0.000 description 1
- 229960000074 biopharmaceutical Drugs 0.000 description 1
- OWMVSZAMULFTJU-UHFFFAOYSA-N bis-tris Chemical compound OCCN(CCO)C(CO)(CO)CO OWMVSZAMULFTJU-UHFFFAOYSA-N 0.000 description 1
- 239000003114 blood coagulation factor Substances 0.000 description 1
- 229960000182 blood factors Drugs 0.000 description 1
- 239000013018 capto adhere resin Substances 0.000 description 1
- 239000012930 cell culture fluid Substances 0.000 description 1
- 239000006143 cell culture medium Substances 0.000 description 1
- 239000013592 cell lysate Substances 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 229960003115 certolizumab pegol Drugs 0.000 description 1
- 239000003638 chemical reducing agent Substances 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 230000001627 detrimental effect Effects 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 206010012601 diabetes mellitus Diseases 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 229940126534 drug product Drugs 0.000 description 1
- 229940088679 drug related substance Drugs 0.000 description 1
- 229940105423 erythropoietin Drugs 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 238000000855 fermentation Methods 0.000 description 1
- 230000004151 fermentation Effects 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 239000012537 formulation buffer Substances 0.000 description 1
- 229960001743 golimumab Drugs 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- 239000013628 high molecular weight specie Substances 0.000 description 1
- 230000028993 immune response Effects 0.000 description 1
- 208000027866 inflammatory disease Diseases 0.000 description 1
- 230000004054 inflammatory process Effects 0.000 description 1
- 229960000598 infliximab Drugs 0.000 description 1
- 229940125396 insulin Drugs 0.000 description 1
- 229940079322 interferon Drugs 0.000 description 1
- 238000005342 ion exchange Methods 0.000 description 1
- VZCYOOQTPOCHFL-UPHRSURJSA-N maleic acid Chemical compound OC(=O)\C=C/C(O)=O VZCYOOQTPOCHFL-UPHRSURJSA-N 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 208000010125 myocardial infarction Diseases 0.000 description 1
- QVRVXSZKCXFBTE-UHFFFAOYSA-N n-[4-(6,7-dimethoxy-3,4-dihydro-1h-isoquinolin-2-yl)butyl]-2-(2-fluoroethoxy)-5-methylbenzamide Chemical compound C1C=2C=C(OC)C(OC)=CC=2CCN1CCCCNC(=O)C1=CC(C)=CC=C1OCCF QVRVXSZKCXFBTE-UHFFFAOYSA-N 0.000 description 1
- 230000009871 nonspecific binding Effects 0.000 description 1
- 229960002446 octanoic acid Drugs 0.000 description 1
- 238000006384 oligomerization reaction Methods 0.000 description 1
- 230000008506 pathogenesis Effects 0.000 description 1
- 230000010412 perfusion Effects 0.000 description 1
- 239000000825 pharmaceutical preparation Substances 0.000 description 1
- 230000004962 physiological condition Effects 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
- OXCMYAYHXIHQOA-UHFFFAOYSA-N potassium;[2-butyl-5-chloro-3-[[4-[2-(1,2,4-triaza-3-azanidacyclopenta-1,4-dien-5-yl)phenyl]phenyl]methyl]imidazol-4-yl]methanol Chemical compound [K+].CCCCC1=NC(Cl)=C(CO)N1CC1=CC=C(C=2C(=CC=CC=2)C2=N[N-]N=N2)C=C1 OXCMYAYHXIHQOA-UHFFFAOYSA-N 0.000 description 1
- 230000003389 potentiating effect Effects 0.000 description 1
- 230000000770 proinflammatory effect Effects 0.000 description 1
- 239000013636 protein dimer Substances 0.000 description 1
- 230000017854 proteolysis Effects 0.000 description 1
- 230000001105 regulatory effect Effects 0.000 description 1
- 229960001886 rilonacept Drugs 0.000 description 1
- 108010046141 rilonacept Proteins 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 238000010186 staining Methods 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 230000001225 therapeutic effect Effects 0.000 description 1
- 238000002560 therapeutic procedure Methods 0.000 description 1
- 239000003053 toxin Substances 0.000 description 1
- 231100000765 toxin Toxicity 0.000 description 1
- 108700012359 toxins Proteins 0.000 description 1
- VZCYOOQTPOCHFL-UHFFFAOYSA-N trans-butenedioic acid Natural products OC(=O)C=CC(O)=O VZCYOOQTPOCHFL-UHFFFAOYSA-N 0.000 description 1
- 239000013638 trimer Substances 0.000 description 1
- 102000003390 tumor necrosis factor Human genes 0.000 description 1
- 229940046728 tumor necrosis factor alpha inhibitor Drugs 0.000 description 1
- 239000002451 tumor necrosis factor inhibitor Substances 0.000 description 1
- 238000000108 ultra-filtration Methods 0.000 description 1
- 238000010977 unit operation Methods 0.000 description 1
- 238000012800 visualization Methods 0.000 description 1
- 238000007805 zymography Methods 0.000 description 1
Classifications
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01D—SEPARATION
- B01D15/00—Separating processes involving the treatment of liquids with solid sorbents; Apparatus therefor
- B01D15/08—Selective adsorption, e.g. chromatography
- B01D15/10—Selective adsorption, e.g. chromatography characterised by constructional or operational features
- B01D15/12—Selective adsorption, e.g. chromatography characterised by constructional or operational features relating to the preparation of the feed
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01D—SEPARATION
- B01D15/00—Separating processes involving the treatment of liquids with solid sorbents; Apparatus therefor
- B01D15/08—Selective adsorption, e.g. chromatography
- B01D15/10—Selective adsorption, e.g. chromatography characterised by constructional or operational features
- B01D15/20—Selective adsorption, e.g. chromatography characterised by constructional or operational features relating to the conditioning of the sorbent material
- B01D15/203—Equilibration or regeneration
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01D—SEPARATION
- B01D15/00—Separating processes involving the treatment of liquids with solid sorbents; Apparatus therefor
- B01D15/08—Selective adsorption, e.g. chromatography
- B01D15/26—Selective adsorption, e.g. chromatography characterised by the separation mechanism
- B01D15/30—Partition chromatography
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01D—SEPARATION
- B01D15/00—Separating processes involving the treatment of liquids with solid sorbents; Apparatus therefor
- B01D15/08—Selective adsorption, e.g. chromatography
- B01D15/26—Selective adsorption, e.g. chromatography characterised by the separation mechanism
- B01D15/36—Selective adsorption, e.g. chromatography characterised by the separation mechanism involving ionic interaction, e.g. ion-exchange, ion-pair, ion-suppression or ion-exclusion
- B01D15/361—Ion-exchange
- B01D15/363—Anion-exchange
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01D—SEPARATION
- B01D15/00—Separating processes involving the treatment of liquids with solid sorbents; Apparatus therefor
- B01D15/08—Selective adsorption, e.g. chromatography
- B01D15/26—Selective adsorption, e.g. chromatography characterised by the separation mechanism
- B01D15/38—Selective adsorption, e.g. chromatography characterised by the separation mechanism involving specific interaction not covered by one or more of groups B01D15/265 and B01D15/30 - B01D15/36, e.g. affinity, ligand exchange or chiral chromatography
- B01D15/3804—Affinity chromatography
- B01D15/3809—Affinity chromatography of the antigen-antibody type, e.g. protein A, G or L chromatography
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01D—SEPARATION
- B01D15/00—Separating processes involving the treatment of liquids with solid sorbents; Apparatus therefor
- B01D15/08—Selective adsorption, e.g. chromatography
- B01D15/26—Selective adsorption, e.g. chromatography characterised by the separation mechanism
- B01D15/38—Selective adsorption, e.g. chromatography characterised by the separation mechanism involving specific interaction not covered by one or more of groups B01D15/265 and B01D15/30 - B01D15/36, e.g. affinity, ligand exchange or chiral chromatography
- B01D15/3847—Multimodal interactions
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01D—SEPARATION
- B01D15/00—Separating processes involving the treatment of liquids with solid sorbents; Apparatus therefor
- B01D15/08—Selective adsorption, e.g. chromatography
- B01D15/42—Selective adsorption, e.g. chromatography characterised by the development mode, e.g. by displacement or by elution
- B01D15/424—Elution mode
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
- C07K14/70578—NGF-receptor/TNF-receptor superfamily, e.g. CD27, CD30, CD40, CD95
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
- C07K14/715—Receptors; Cell surface antigens; Cell surface determinants for cytokines; for lymphokines; for interferons
- C07K14/7151—Receptors; Cell surface antigens; Cell surface determinants for cytokines; for lymphokines; for interferons for tumor necrosis factor [TNF], for lymphotoxin [LT]
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/30—Non-immunoglobulin-derived peptide or protein having an immunoglobulin constant or Fc region, or a fragment thereof, attached thereto
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Analytical Chemistry (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Organic Chemistry (AREA)
- Immunology (AREA)
- Molecular Biology (AREA)
- Gastroenterology & Hepatology (AREA)
- Zoology (AREA)
- Toxicology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Cell Biology (AREA)
- Peptides Or Proteins (AREA)
- Enzymes And Modification Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| IN1919MU2014 | 2014-06-13 | ||
| IN1919/MUM/2014 | 2014-06-13 | ||
| PCT/IB2015/054494 WO2015189832A1 (en) | 2014-06-13 | 2015-06-13 | Process for the purification of tnfr:fc fusion protein |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA2951766A1 true CA2951766A1 (en) | 2015-12-17 |
Family
ID=53524922
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA2951766A Abandoned CA2951766A1 (en) | 2014-06-13 | 2015-06-13 | Process for the purification of tnfr:fc fusion protein |
Country Status (12)
| Country | Link |
|---|---|
| US (1) | US10556942B2 (enExample) |
| EP (1) | EP3155009A1 (enExample) |
| JP (1) | JP6747985B2 (enExample) |
| CN (1) | CN106536565A (enExample) |
| AU (1) | AU2015273049B2 (enExample) |
| BR (1) | BR112016029157A8 (enExample) |
| CA (1) | CA2951766A1 (enExample) |
| MA (1) | MA40232A (enExample) |
| MX (1) | MX2016016318A (enExample) |
| PH (1) | PH12016502482A1 (enExample) |
| RU (1) | RU2698654C2 (enExample) |
| WO (1) | WO2015189832A1 (enExample) |
Families Citing this family (26)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US11566082B2 (en) | 2014-11-17 | 2023-01-31 | Cytiva Bioprocess R&D Ab | Mutated immunoglobulin-binding polypeptides |
| KR20170138426A (ko) * | 2015-03-13 | 2017-12-15 | 삼성바이오에피스 주식회사 | 항-tnf-알파 폴리펩티드 조성물 및 그 용도 |
| WO2017194592A1 (en) | 2016-05-11 | 2017-11-16 | Ge Healthcare Bioprocess R&D Ab | Method of storing a separation matrix |
| US10889615B2 (en) | 2016-05-11 | 2021-01-12 | Cytiva Bioprocess R&D Ab | Mutated immunoglobulin-binding polypeptides |
| US11753438B2 (en) | 2016-05-11 | 2023-09-12 | Cytiva Bioprocess R&D Ab | Method of cleaning and/or sanitizing a separation matrix |
| US10703774B2 (en) | 2016-09-30 | 2020-07-07 | Ge Healthcare Bioprocess R&D Ab | Separation method |
| US10730908B2 (en) | 2016-05-11 | 2020-08-04 | Ge Healthcare Bioprocess R&D Ab | Separation method |
| CN109071613A (zh) | 2016-05-11 | 2018-12-21 | 通用电气医疗集团生物工艺研发股份公司 | 分离基质 |
| JP7031934B2 (ja) | 2016-05-11 | 2022-03-08 | サイティバ・バイオプロセス・アールアンドディ・アクチボラグ | 分離マトリックス |
| US10654887B2 (en) | 2016-05-11 | 2020-05-19 | Ge Healthcare Bio-Process R&D Ab | Separation matrix |
| US12448411B2 (en) | 2016-09-30 | 2025-10-21 | Cytiva Bioprocess R&D Ab | Separation method |
| EP3668985B1 (en) * | 2017-08-17 | 2021-06-16 | Just-Evotec Biologics, Inc. | Method of purifying glycosylated protein from host cell galectins and other contaminants |
| EP3676281A1 (en) * | 2017-08-30 | 2020-07-08 | Ares Trading S.A. | Method for purifying proteins |
| US11952399B2 (en) * | 2018-12-18 | 2024-04-09 | Amgen Inc. | Methods for purifying proteins |
| JP2022523063A (ja) * | 2019-01-30 | 2022-04-21 | アムジエン・インコーポレーテツド | アフリベルセプトの属性、並びにその特性決定及び修飾方法 |
| KR102286892B1 (ko) * | 2019-07-08 | 2021-08-06 | 삼천당제약주식회사 | 안과용 단백질 제제의 정제방법 |
| CN112876567A (zh) * | 2019-11-29 | 2021-06-01 | 广东菲鹏制药股份有限公司 | Fc融合蛋白及其纯化方法 |
| US20230357315A1 (en) * | 2020-03-11 | 2023-11-09 | Dr. Reddy's Laboratories Limited | METHOD OF PURIFYING AN Fc-FUSION PROTEIN |
| CN113563469A (zh) * | 2020-04-28 | 2021-10-29 | 江苏中新医药有限公司 | 高回收率纯化阿达木单抗的方法 |
| WO2022234412A1 (en) * | 2021-05-03 | 2022-11-10 | Lupin Limited | A process for purification of fc-fusion proteins |
| WO2023053032A1 (en) * | 2021-09-28 | 2023-04-06 | Kashiv Biosciences, Llc | An improved process for purification of fusion protein |
| WO2023053030A1 (en) * | 2021-09-28 | 2023-04-06 | Kashiv Biosciences, Llc | An improved process for purification of protein |
| AU2022358612A1 (en) * | 2021-09-28 | 2024-04-11 | Kashiv Biosciences, Llc | An improved process of purification of fusion protein |
| MX2024004764A (es) * | 2021-10-19 | 2024-07-04 | Alteogen Inc | Procedimiento para purificar una proteína de fusión que tiene un dominio fc de igg. |
| EP4435107A4 (en) * | 2021-11-29 | 2025-12-31 | Tosoh Corp | ANTIBODY ISOLATION METHOD |
| CN119060168A (zh) * | 2024-09-26 | 2024-12-03 | 广东丸美生物技术股份有限公司 | 一种具有低电导率的重组胶原蛋白溶液及其制备方法和应用 |
Family Cites Families (20)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| RU2021284C1 (ru) * | 1991-05-30 | 1994-10-15 | Всесоюзный научно-исследовательский институт технологии кровезаменителей и гормональных препаратов | Способ очистки клинических фракций декстрана |
| US7294481B1 (en) | 1999-01-05 | 2007-11-13 | Immunex Corporation | Method for producing recombinant proteins |
| MXPA04008215A (es) | 2002-02-27 | 2004-11-26 | Immunex Corp | Formulacion polipeptidica. |
| AU2004215653B2 (en) | 2003-02-28 | 2011-03-17 | Lonza Biologics Plc. | Antibody purification by protein A and ion exchange chromatography |
| US8263750B2 (en) * | 2006-03-16 | 2012-09-11 | Amgen Inc. | Method for purifying a protein using protein-A affinity chromatography using an intermediate wash step |
| JP2010501622A (ja) * | 2006-08-28 | 2010-01-21 | アレス トレーディング ソシエテ アノニム | Ｆｃ−融合タンパク質の精製法 |
| ES2755386T5 (es) * | 2006-08-28 | 2023-04-05 | Ares Trading Sa | Proceso para la purificación de proteínas que contienen fragmentos Fc |
| US20100256337A1 (en) | 2007-10-22 | 2010-10-07 | Merck Serono Sa | Method for purifying an fc-containing protein |
| WO2009111347A1 (en) * | 2008-02-29 | 2009-09-11 | Biogen Idec Ma Inc. | Purified immunoglobulin fusion proteins and methods of their purification |
| KR20110079693A (ko) * | 2008-10-29 | 2011-07-07 | 와이어쓰 엘엘씨 | 단일 도메인 항원 결합 분자의 정제 방법 |
| EP2526114B1 (de) * | 2010-01-22 | 2014-06-18 | Boehringer Ingelheim International GmbH | Chromatographisches verfahren zur aufreinigung von fc enthaltenden proteinen |
| WO2012176158A1 (en) * | 2011-06-24 | 2012-12-27 | Dr. Reddy's Laboratories Limited | Purification of chimeric protein |
| AU2012282960A1 (en) * | 2011-07-08 | 2014-01-16 | Merck Sharp & Dohme Corp. | Method for purifying Fc-fusion protein |
| JP6223338B2 (ja) * | 2011-08-17 | 2017-11-01 | アレス トレーディング ソシエテ アノニム | 活性型ＴＮＦＲ−Ｆｃ融合タンパク質を製造する方法 |
| US9249182B2 (en) | 2012-05-24 | 2016-02-02 | Abbvie, Inc. | Purification of antibodies using hydrophobic interaction chromatography |
| SG11201501460RA (en) * | 2012-09-11 | 2015-04-29 | Coherus Biosciences Inc | Correctly folded etanercept in high purity and excellent yield |
| CN102911250B (zh) * | 2012-09-29 | 2014-04-16 | 浙江海正药业股份有限公司 | 酸性重组蛋白药物的纯化方法 |
| EP2919812A4 (en) * | 2012-11-19 | 2016-05-18 | Merck Sharp & Dohme | Liquid formulations for TNFR: FC fusion proteins |
| ES2964601T3 (es) * | 2013-03-14 | 2024-04-08 | Amgen Inc | Eliminación de ligando de purificación por afinidad filtrado |
| US8946395B1 (en) * | 2013-10-18 | 2015-02-03 | Abbvie Inc. | Purification of proteins using hydrophobic interaction chromatography |
-
2015
- 2015-06-13 EP EP15734731.1A patent/EP3155009A1/en not_active Withdrawn
- 2015-06-13 CN CN201580038801.XA patent/CN106536565A/zh active Pending
- 2015-06-13 BR BR112016029157A patent/BR112016029157A8/pt not_active Application Discontinuation
- 2015-06-13 CA CA2951766A patent/CA2951766A1/en not_active Abandoned
- 2015-06-13 WO PCT/IB2015/054494 patent/WO2015189832A1/en not_active Ceased
- 2015-06-13 MX MX2016016318A patent/MX2016016318A/es unknown
- 2015-06-13 JP JP2016572703A patent/JP6747985B2/ja not_active Expired - Fee Related
- 2015-06-13 US US15/318,489 patent/US10556942B2/en active Active
- 2015-06-13 AU AU2015273049A patent/AU2015273049B2/en not_active Ceased
- 2015-06-13 RU RU2017100005A patent/RU2698654C2/ru active
- 2015-06-13 MA MA040232A patent/MA40232A/fr unknown
-
2016
- 2016-12-13 PH PH12016502482A patent/PH12016502482A1/en unknown
Also Published As
| Publication number | Publication date |
|---|---|
| MX2016016318A (es) | 2017-06-12 |
| US20170152298A1 (en) | 2017-06-01 |
| EP3155009A1 (en) | 2017-04-19 |
| US10556942B2 (en) | 2020-02-11 |
| JP6747985B2 (ja) | 2020-08-26 |
| MA40232A (fr) | 2017-04-19 |
| AU2015273049A1 (en) | 2017-01-12 |
| JP2017521389A (ja) | 2017-08-03 |
| AU2015273049B2 (en) | 2019-11-14 |
| RU2017100005A3 (enExample) | 2019-02-28 |
| WO2015189832A1 (en) | 2015-12-17 |
| CN106536565A (zh) | 2017-03-22 |
| BR112016029157A8 (pt) | 2021-07-06 |
| RU2017100005A (ru) | 2018-07-13 |
| RU2698654C2 (ru) | 2019-08-28 |
| PH12016502482A1 (en) | 2017-04-10 |
| BR112016029157A2 (pt) | 2017-08-22 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| AU2015273049B2 (en) | Process for the purification of TNFR:Fc fusion protein | |
| KR101683415B1 (ko) | 단일클론항체에 대한 정제 방법 | |
| CN102712673B (zh) | 用于纯化含fc的蛋白的色谱方法 | |
| EP2791176B1 (en) | A method of antibody purification | |
| CN105777904B (zh) | 抗TNFα类单克隆抗体的阳离子交换色谱纯化方法 | |
| US20120202974A1 (en) | Process for the purification of fc-containing proteins | |
| RU2590726C2 (ru) | Способ очистки витамин к-зависимых белков, таких как коагуляционный фактор ix | |
| CN113710685B (zh) | 通过使用捕获前的絮凝改善免疫球蛋白的亲和色谱 | |
| NZ574623A (en) | Process for the purification of fc-fusion proteins | |
| CN102911250B (zh) | 酸性重组蛋白药物的纯化方法 | |
| CA3182368A1 (en) | An improved process of purification of protein | |
| JP2023139142A (ja) | 眼科用タンパク質医薬品の精製方法（Ｒｅｆｉｎｉｎｇ ｍｅｔｈｏｄ ｏｆ ｏｐｈｔｈａｌｍｉｃ ｐｒｏｔｅｉｎ ｐｈａｒｍａｃｅｕｔｉｃａｌｓ） | |
| EP4408856A1 (en) | An improved process for purification of protein | |
| NZ574626A (en) | Process for removing free Fc-moieties from fluids comprising Fc-containing proteins using ion exchange chromatography | |
| CN105777903B (zh) | 一种阿达木单抗的阳离子交换色谱纯化方法 | |
| KR20070091098A (ko) | 단백질 분리 방법 | |
| WO2022234412A1 (en) | A process for purification of fc-fusion proteins | |
| WO2025219869A1 (en) | Methods of purifying immunoglobulins comprising n-terminal glutamine | |
| CN118291432A (zh) | 一种利用非亲和层析捕获技术纯化蛋白的方法 | |
| HK1174044B (en) | Chromatographic method for purifying fc-containing proteins |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| EEER | Examination request |
Effective date: 20200602 |
|
| FZDE | Discontinued |
Effective date: 20220920 |
|
| FZDE | Discontinued |
Effective date: 20220920 |