DK2994485T3 - CONTINUOUS MULTIPLE STEP PROCEDURE FOR PURIFICATION OF ANTIBODIES - Google Patents
CONTINUOUS MULTIPLE STEP PROCEDURE FOR PURIFICATION OF ANTIBODIES Download PDFInfo
- Publication number
- DK2994485T3 DK2994485T3 DK14722194.9T DK14722194T DK2994485T3 DK 2994485 T3 DK2994485 T3 DK 2994485T3 DK 14722194 T DK14722194 T DK 14722194T DK 2994485 T3 DK2994485 T3 DK 2994485T3
- Authority
- DK
- Denmark
- Prior art keywords
- chromatography column
- chromatography
- protein
- over
- passing
- Prior art date
Links
- 238000000034 method Methods 0.000 title claims abstract description 231
- 238000000746 purification Methods 0.000 title abstract description 44
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 239
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 239
- 238000004587 chromatography analysis Methods 0.000 claims abstract description 190
- 230000008569 process Effects 0.000 claims abstract description 50
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 claims description 226
- 238000011210 chromatographic step Methods 0.000 claims description 115
- 239000000872 buffer Substances 0.000 claims description 99
- 239000000243 solution Substances 0.000 claims description 91
- OWMVSZAMULFTJU-UHFFFAOYSA-N bis-tris Chemical compound OCCN(CCO)C(CO)(CO)CO OWMVSZAMULFTJU-UHFFFAOYSA-N 0.000 claims description 87
- 239000012149 elution buffer Substances 0.000 claims description 87
- 239000006167 equilibration buffer Substances 0.000 claims description 86
- 239000011347 resin Substances 0.000 claims description 82
- 229920005989 resin Polymers 0.000 claims description 82
- 235000019750 Crude protein Nutrition 0.000 claims description 46
- 239000003480 eluent Substances 0.000 claims description 45
- 239000011534 wash buffer Substances 0.000 claims description 41
- 238000005571 anion exchange chromatography Methods 0.000 claims description 34
- 238000001728 nano-filtration Methods 0.000 claims description 27
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 23
- 241000282414 Homo sapiens Species 0.000 claims description 15
- 238000001042 affinity chromatography Methods 0.000 claims description 13
- 239000000463 material Substances 0.000 claims description 11
- 238000010979 pH adjustment Methods 0.000 claims description 8
- 238000010790 dilution Methods 0.000 claims description 7
- 239000012895 dilution Substances 0.000 claims description 7
- 238000011282 treatment Methods 0.000 claims description 7
- 238000013060 ultrafiltration and diafiltration Methods 0.000 claims description 7
- 102100031585 ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1 Human genes 0.000 claims description 6
- 102100025475 Carcinoembryonic antigen-related cell adhesion molecule 5 Human genes 0.000 claims description 6
- 101710190849 Carcinoembryonic antigen-related cell adhesion molecule 5 Proteins 0.000 claims description 6
- 101000777636 Homo sapiens ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1 Proteins 0.000 claims description 6
- 102100023935 Transmembrane glycoprotein NMB Human genes 0.000 claims description 5
- 230000001580 bacterial effect Effects 0.000 claims description 5
- 108091007466 transmembrane glycoproteins Proteins 0.000 claims description 5
- 239000008194 pharmaceutical composition Substances 0.000 claims description 4
- 102000013455 Amyloid beta-Peptides Human genes 0.000 claims description 3
- 108010090849 Amyloid beta-Peptides Proteins 0.000 claims description 3
- OVRNDRQMDRJTHS-FMDGEEDCSA-N N-acetyl-beta-D-glucosamine Chemical compound CC(=O)N[C@H]1[C@H](O)O[C@H](CO)[C@@H](O)[C@@H]1O OVRNDRQMDRJTHS-FMDGEEDCSA-N 0.000 claims description 3
- 150000004676 glycans Chemical class 0.000 claims description 3
- 229950006780 n-acetylglucosamine Drugs 0.000 claims description 3
- 229920001282 polysaccharide Polymers 0.000 claims description 3
- 239000005017 polysaccharide Substances 0.000 claims description 3
- 238000011084 recovery Methods 0.000 claims description 3
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 claims 12
- 239000011780 sodium chloride Substances 0.000 claims 6
- 239000010413 mother solution Substances 0.000 abstract description 9
- 239000007853 buffer solution Substances 0.000 abstract description 3
- 235000018102 proteins Nutrition 0.000 description 223
- 239000012528 membrane Substances 0.000 description 184
- 239000012504 chromatography matrix Substances 0.000 description 112
- 239000012530 fluid Substances 0.000 description 30
- 238000005341 cation exchange Methods 0.000 description 22
- 239000013017 sartobind Substances 0.000 description 20
- 230000027455 binding Effects 0.000 description 16
- 239000001963 growth medium Substances 0.000 description 16
- 239000003011 anion exchange membrane Substances 0.000 description 14
- 238000003860 storage Methods 0.000 description 14
- 230000002779 inactivation Effects 0.000 description 13
- 239000011159 matrix material Substances 0.000 description 13
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 12
- 238000005277 cation exchange chromatography Methods 0.000 description 12
- 238000005352 clarification Methods 0.000 description 12
- 239000012535 impurity Substances 0.000 description 12
- 238000009630 liquid culture Methods 0.000 description 12
- 230000007246 mechanism Effects 0.000 description 12
- 238000010828 elution Methods 0.000 description 11
- 239000000203 mixture Substances 0.000 description 10
- 230000008901 benefit Effects 0.000 description 9
- 210000004027 cell Anatomy 0.000 description 9
- 238000001914 filtration Methods 0.000 description 9
- 238000000108 ultra-filtration Methods 0.000 description 9
- 238000011026 diafiltration Methods 0.000 description 8
- 230000003993 interaction Effects 0.000 description 8
- 238000011067 equilibration Methods 0.000 description 7
- 238000003306 harvesting Methods 0.000 description 7
- 229920001184 polypeptide Polymers 0.000 description 7
- 102000004196 processed proteins & peptides Human genes 0.000 description 7
- 108090000765 processed proteins & peptides Proteins 0.000 description 7
- 150000003839 salts Chemical class 0.000 description 7
- 241000700605 Viruses Species 0.000 description 6
- 230000002378 acidificating effect Effects 0.000 description 6
- 238000002474 experimental method Methods 0.000 description 6
- 239000012467 final product Substances 0.000 description 6
- 239000012634 fragment Substances 0.000 description 6
- 230000003612 virological effect Effects 0.000 description 6
- 150000001413 amino acids Chemical class 0.000 description 5
- 239000000427 antigen Substances 0.000 description 5
- 108091007433 antigens Proteins 0.000 description 5
- 102000036639 antigens Human genes 0.000 description 5
- 235000009508 confectionery Nutrition 0.000 description 5
- 238000013400 design of experiment Methods 0.000 description 5
- 238000005457 optimization Methods 0.000 description 5
- 238000005498 polishing Methods 0.000 description 5
- 238000010977 unit operation Methods 0.000 description 5
- ZNIFSRGNXRYGHF-UHFFFAOYSA-N Clonidine hydrochloride Chemical compound Cl.ClC1=CC=CC(Cl)=C1NC1=NCCN1 ZNIFSRGNXRYGHF-UHFFFAOYSA-N 0.000 description 4
- 238000004458 analytical method Methods 0.000 description 4
- 238000004113 cell culture Methods 0.000 description 4
- 238000010924 continuous production Methods 0.000 description 4
- 238000009295 crossflow filtration Methods 0.000 description 4
- 239000012071 phase Substances 0.000 description 4
- 238000002360 preparation method Methods 0.000 description 4
- 239000000047 product Substances 0.000 description 4
- 238000005070 sampling Methods 0.000 description 4
- 238000013341 scale-up Methods 0.000 description 4
- 102100026189 Beta-galactosidase Human genes 0.000 description 3
- -1 NaCI Chemical compound 0.000 description 3
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 3
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 3
- 239000003957 anion exchange resin Substances 0.000 description 3
- 108010005774 beta-Galactosidase Proteins 0.000 description 3
- 238000004440 column chromatography Methods 0.000 description 3
- 238000011109 contamination Methods 0.000 description 3
- 230000006870 function Effects 0.000 description 3
- 230000000415 inactivating effect Effects 0.000 description 3
- 239000007788 liquid Substances 0.000 description 3
- 238000004519 manufacturing process Methods 0.000 description 3
- 239000002245 particle Substances 0.000 description 3
- 238000001742 protein purification Methods 0.000 description 3
- 210000005253 yeast cell Anatomy 0.000 description 3
- NLXLAEXVIDQMFP-UHFFFAOYSA-N Ammonia chloride Chemical compound [NH4+].[Cl-] NLXLAEXVIDQMFP-UHFFFAOYSA-N 0.000 description 2
- 241000894006 Bacteria Species 0.000 description 2
- 102000004190 Enzymes Human genes 0.000 description 2
- 108090000790 Enzymes Proteins 0.000 description 2
- 108060003951 Immunoglobulin Proteins 0.000 description 2
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 2
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 2
- 239000012515 MabSelect SuRe Substances 0.000 description 2
- 241000270276 Natrix Species 0.000 description 2
- 239000007983 Tris buffer Substances 0.000 description 2
- 108060008682 Tumor Necrosis Factor Proteins 0.000 description 2
- 238000002835 absorbance Methods 0.000 description 2
- 108010070626 acid beta-galactosidase Proteins 0.000 description 2
- 125000000129 anionic group Chemical group 0.000 description 2
- 238000011091 antibody purification Methods 0.000 description 2
- 238000011095 buffer preparation Methods 0.000 description 2
- 150000001875 compounds Chemical class 0.000 description 2
- 238000011437 continuous method Methods 0.000 description 2
- 238000013461 design Methods 0.000 description 2
- 238000011143 downstream manufacturing Methods 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 238000009472 formulation Methods 0.000 description 2
- 230000036541 health Effects 0.000 description 2
- 238000009396 hybridization Methods 0.000 description 2
- 230000002209 hydrophobic effect Effects 0.000 description 2
- 230000001900 immune effect Effects 0.000 description 2
- 102000018358 immunoglobulin Human genes 0.000 description 2
- 238000000338 in vitro Methods 0.000 description 2
- 238000001727 in vivo Methods 0.000 description 2
- NDDAHWYSQHTHNT-UHFFFAOYSA-N indapamide Chemical compound CC1CC2=CC=CC=C2N1NC(=O)C1=CC=C(Cl)C(S(N)(=O)=O)=C1 NDDAHWYSQHTHNT-UHFFFAOYSA-N 0.000 description 2
- 238000011068 loading method Methods 0.000 description 2
- 230000007774 longterm Effects 0.000 description 2
- 230000014759 maintenance of location Effects 0.000 description 2
- 238000012544 monitoring process Methods 0.000 description 2
- 229960001972 panitumumab Drugs 0.000 description 2
- 230000010412 perfusion Effects 0.000 description 2
- 230000000737 periodic effect Effects 0.000 description 2
- 235000004252 protein component Nutrition 0.000 description 2
- 239000002994 raw material Substances 0.000 description 2
- 230000009467 reduction Effects 0.000 description 2
- 230000004044 response Effects 0.000 description 2
- 210000001082 somatic cell Anatomy 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 230000001225 therapeutic effect Effects 0.000 description 2
- 229960003989 tocilizumab Drugs 0.000 description 2
- 230000009466 transformation Effects 0.000 description 2
- 239000008215 water for injection Substances 0.000 description 2
- 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
- NFGXHKASABOEEW-UHFFFAOYSA-N 1-methylethyl 11-methoxy-3,7,11-trimethyl-2,4-dodecadienoate Chemical compound COC(C)(C)CCCC(C)CC=CC(C)=CC(=O)OC(C)C NFGXHKASABOEEW-UHFFFAOYSA-N 0.000 description 1
- 102000006772 Acid Ceramidase Human genes 0.000 description 1
- 108020005296 Acid Ceramidase Proteins 0.000 description 1
- 229920000936 Agarose Polymers 0.000 description 1
- 108091023037 Aptamer Proteins 0.000 description 1
- 101100454807 Caenorhabditis elegans lgg-1 gene Proteins 0.000 description 1
- 101100454808 Caenorhabditis elegans lgg-2 gene Proteins 0.000 description 1
- 101100217502 Caenorhabditis elegans lgg-3 gene Proteins 0.000 description 1
- 108010047041 Complementarity Determining Regions Proteins 0.000 description 1
- 101100276976 Drosophila melanogaster Drak gene Proteins 0.000 description 1
- 108010008165 Etanercept Proteins 0.000 description 1
- 102100028496 Galactocerebrosidase Human genes 0.000 description 1
- 108010042681 Galactosylceramidase Proteins 0.000 description 1
- 108010053317 Hexosaminidase A Proteins 0.000 description 1
- 102000016871 Hexosaminidase A Human genes 0.000 description 1
- 108010053345 Hexosaminidase B Proteins 0.000 description 1
- 102000016870 Hexosaminidase B Human genes 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 101000987586 Homo sapiens Eosinophil peroxidase Proteins 0.000 description 1
- 101000920686 Homo sapiens Erythropoietin Proteins 0.000 description 1
- 108010053927 Iduronate Sulfatase Proteins 0.000 description 1
- 102000004627 Iduronidase Human genes 0.000 description 1
- 108010003381 Iduronidase Proteins 0.000 description 1
- 102000006992 Interferon-alpha Human genes 0.000 description 1
- 108010047761 Interferon-alpha Proteins 0.000 description 1
- 102000003996 Interferon-beta Human genes 0.000 description 1
- 108090000467 Interferon-beta Proteins 0.000 description 1
- 102000004083 Lymphotoxin-alpha Human genes 0.000 description 1
- 108090000542 Lymphotoxin-alpha Proteins 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 241001529936 Murinae Species 0.000 description 1
- 102000005348 Neuraminidase Human genes 0.000 description 1
- 108010006232 Neuraminidase Proteins 0.000 description 1
- 239000004696 Poly ether ether ketone Substances 0.000 description 1
- 108010061312 Sphingomyelin Phosphodiesterase Proteins 0.000 description 1
- 102000000019 Sterol Esterase Human genes 0.000 description 1
- 108010055297 Sterol Esterase Proteins 0.000 description 1
- 101710120037 Toxin CcdB Proteins 0.000 description 1
- 102100040247 Tumor necrosis factor Human genes 0.000 description 1
- 108010044965 UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase Proteins 0.000 description 1
- 229950005186 abagovomab Drugs 0.000 description 1
- 229960000446 abciximab Drugs 0.000 description 1
- 239000002250 absorbent Substances 0.000 description 1
- 230000002745 absorbent Effects 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 102000010126 acid sphingomyelin phosphodiesterase activity proteins Human genes 0.000 description 1
- 229950004283 actoxumab Drugs 0.000 description 1
- 229960002964 adalimumab Drugs 0.000 description 1
- 238000007792 addition Methods 0.000 description 1
- 229950009084 adecatumumab Drugs 0.000 description 1
- 229960003227 afelimomab Drugs 0.000 description 1
- 229960000548 alemtuzumab Drugs 0.000 description 1
- 229960004539 alirocumab Drugs 0.000 description 1
- 229950009106 altumomab Drugs 0.000 description 1
- 229950001537 amatuximab Drugs 0.000 description 1
- 235000019270 ammonium chloride Nutrition 0.000 description 1
- 238000005349 anion exchange Methods 0.000 description 1
- 230000000890 antigenic effect Effects 0.000 description 1
- 229950003145 apolizumab Drugs 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 229950005122 atinumab Drugs 0.000 description 1
- 238000010923 batch production Methods 0.000 description 1
- 229950003269 bectumomab Drugs 0.000 description 1
- 229960003270 belimumab Drugs 0.000 description 1
- JUPQTSLXMOCDHR-UHFFFAOYSA-N benzene-1,4-diol;bis(4-fluorophenyl)methanone Chemical group OC1=CC=C(O)C=C1.C1=CC(F)=CC=C1C(=O)C1=CC=C(F)C=C1 JUPQTSLXMOCDHR-UHFFFAOYSA-N 0.000 description 1
- 102000006995 beta-Glucosidase Human genes 0.000 description 1
- 108010047754 beta-Glucosidase Proteins 0.000 description 1
- 229960000397 bevacizumab Drugs 0.000 description 1
- 229950001303 biciromab Drugs 0.000 description 1
- 230000001588 bifunctional effect Effects 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 229960001838 canakinumab Drugs 0.000 description 1
- 239000003729 cation exchange resin Substances 0.000 description 1
- 125000002091 cationic group Chemical group 0.000 description 1
- 150000001768 cations Chemical class 0.000 description 1
- 229960005395 cetuximab Drugs 0.000 description 1
- 239000002131 composite material Substances 0.000 description 1
- 239000000356 contaminant Substances 0.000 description 1
- 238000004185 countercurrent chromatography Methods 0.000 description 1
- 210000004748 cultured cell Anatomy 0.000 description 1
- 229960002806 daclizumab Drugs 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 238000012217 deletion Methods 0.000 description 1
- 230000037430 deletion Effects 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 230000001627 detrimental effect Effects 0.000 description 1
- 238000009792 diffusion process Methods 0.000 description 1
- 238000007865 diluting Methods 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- 229950003468 dupilumab Drugs 0.000 description 1
- 229960002224 eculizumab Drugs 0.000 description 1
- 229960001776 edrecolomab Drugs 0.000 description 1
- 229960000284 efalizumab Drugs 0.000 description 1
- 239000012636 effector Substances 0.000 description 1
- 229950002209 efungumab Drugs 0.000 description 1
- 229950008579 ertumaxomab Drugs 0.000 description 1
- 229960000403 etanercept Drugs 0.000 description 1
- 229950009569 etaracizumab Drugs 0.000 description 1
- 229950004003 fresolimumab Drugs 0.000 description 1
- 238000003055 full factorial design Methods 0.000 description 1
- 125000000524 functional group Chemical group 0.000 description 1
- 238000001641 gel filtration chromatography Methods 0.000 description 1
- 230000013595 glycosylation Effects 0.000 description 1
- 238000006206 glycosylation reaction Methods 0.000 description 1
- 229960001743 golimumab Drugs 0.000 description 1
- 108010089932 heparan sulfate sulfatase Proteins 0.000 description 1
- 239000013628 high molecular weight specie Substances 0.000 description 1
- 102000044890 human EPO Human genes 0.000 description 1
- 229910052739 hydrogen Inorganic materials 0.000 description 1
- 239000001257 hydrogen Substances 0.000 description 1
- 238000004191 hydrophobic interaction chromatography Methods 0.000 description 1
- 230000016784 immunoglobulin production Effects 0.000 description 1
- 229960000598 infliximab Drugs 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- 229960001388 interferon-beta Drugs 0.000 description 1
- 238000004255 ion exchange chromatography Methods 0.000 description 1
- 125000003010 ionic group Chemical group 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- 239000003446 ligand Substances 0.000 description 1
- 238000012417 linear regression Methods 0.000 description 1
- 239000002609 medium Substances 0.000 description 1
- 239000002808 molecular sieve Substances 0.000 description 1
- 229960005027 natalizumab Drugs 0.000 description 1
- 229960003347 obinutuzumab Drugs 0.000 description 1
- 229960000470 omalizumab Drugs 0.000 description 1
- 230000006548 oncogenic transformation Effects 0.000 description 1
- 238000012856 packing Methods 0.000 description 1
- 229960000402 palivizumab Drugs 0.000 description 1
- 239000013618 particulate matter Substances 0.000 description 1
- 230000002572 peristaltic effect Effects 0.000 description 1
- 229960002087 pertuzumab Drugs 0.000 description 1
- 239000008177 pharmaceutical agent Substances 0.000 description 1
- 229920000058 polyacrylate Polymers 0.000 description 1
- 229920002530 polyetherether ketone Polymers 0.000 description 1
- 239000011148 porous material Substances 0.000 description 1
- 230000004481 post-translational protein modification Effects 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
- 230000001737 promoting effect Effects 0.000 description 1
- 238000003908 quality control method Methods 0.000 description 1
- 229960003876 ranibizumab Drugs 0.000 description 1
- 229960000160 recombinant therapeutic protein Drugs 0.000 description 1
- 229960004641 rituximab Drugs 0.000 description 1
- 238000011012 sanitization Methods 0.000 description 1
- 229950006348 sarilumab Drugs 0.000 description 1
- 238000003998 size exclusion chromatography high performance liquid chromatography Methods 0.000 description 1
- URGAHOPLAPQHLN-UHFFFAOYSA-N sodium aluminosilicate Chemical compound [Na+].[Al+3].[O-][Si]([O-])=O.[O-][Si]([O-])=O URGAHOPLAPQHLN-UHFFFAOYSA-N 0.000 description 1
- 239000007790 solid phase Substances 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 239000002594 sorbent Substances 0.000 description 1
- 230000009870 specific binding Effects 0.000 description 1
- 238000006467 substitution reaction Methods 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 230000014723 transformation of host cell by virus Effects 0.000 description 1
- 229960000575 trastuzumab Drugs 0.000 description 1
- 230000001960 triggered effect Effects 0.000 description 1
- 102000003390 tumor necrosis factor Human genes 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/06—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies from serum
- C07K16/065—Purification, fragmentation
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/14—Extraction; Separation; Purification
- C07K1/16—Extraction; Separation; Purification by chromatography
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/14—Extraction; Separation; Purification
- C07K1/36—Extraction; Separation; Purification by a combination of two or more processes of different types
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/06—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies from serum
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/40—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against enzymes
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12M—APPARATUS FOR ENZYMOLOGY OR MICROBIOLOGY; APPARATUS FOR CULTURING MICROORGANISMS FOR PRODUCING BIOMASS, FOR GROWING CELLS OR FOR OBTAINING FERMENTATION OR METABOLIC PRODUCTS, i.e. BIOREACTORS OR FERMENTERS
- C12M47/00—Means for after-treatment of the produced biomass or of the fermentation or metabolic products, e.g. storage of biomass
- C12M47/12—Purification
Landscapes
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Genetics & Genomics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- Medicinal Chemistry (AREA)
- Biophysics (AREA)
- Engineering & Computer Science (AREA)
- Immunology (AREA)
- Analytical Chemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Biotechnology (AREA)
- Sustainable Development (AREA)
- Biomedical Technology (AREA)
- Microbiology (AREA)
- General Engineering & Computer Science (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Oncology (AREA)
- Cell Biology (AREA)
- Water Supply & Treatment (AREA)
- Treatment Of Liquids With Adsorbents In General (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP13305593 | 2013-05-06 | ||
| PCT/EP2014/059246 WO2014180852A1 (en) | 2013-05-06 | 2014-05-06 | Continuous multistep process for purifying antibodies |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| DK2994485T3 true DK2994485T3 (en) | 2018-04-23 |
Family
ID=48430636
Family Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| DK14722194.9T DK2994485T3 (en) | 2013-05-06 | 2014-05-06 | CONTINUOUS MULTIPLE STEP PROCEDURE FOR PURIFICATION OF ANTIBODIES |
| DK17200909.4T DK3301115T3 (da) | 2013-05-06 | 2014-05-06 | Kontinuerlig flertrinsfremgangsmåde til oprensning af antistoffer |
Family Applications After (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| DK17200909.4T DK3301115T3 (da) | 2013-05-06 | 2014-05-06 | Kontinuerlig flertrinsfremgangsmåde til oprensning af antistoffer |
Country Status (19)
Families Citing this family (36)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US9458450B2 (en) | 2012-03-15 | 2016-10-04 | Flodesign Sonics, Inc. | Acoustophoretic separation technology using multi-dimensional standing waves |
| US10704021B2 (en) | 2012-03-15 | 2020-07-07 | Flodesign Sonics, Inc. | Acoustic perfusion devices |
| US10967298B2 (en) | 2012-03-15 | 2021-04-06 | Flodesign Sonics, Inc. | Driver and control for variable impedence load |
| US9950282B2 (en) | 2012-03-15 | 2018-04-24 | Flodesign Sonics, Inc. | Electronic configuration and control for acoustic standing wave generation |
| DK2911759T3 (da) * | 2012-10-24 | 2024-09-16 | Genzyme Corp | Eluering af biomolekyler fra multimodale harpikser under anvendelse af mes og mops som modifikatorer af den mobile fase |
| US10519195B2 (en) * | 2013-09-17 | 2019-12-31 | Kaneka Corporation | Antibody purification method, antibody obtained therefrom, novel antibody purification method using cation exchanger, and antibody obtained therefrom |
| EP3092049A1 (en) | 2014-01-08 | 2016-11-16 | Flodesign Sonics Inc. | Acoustophoresis device with dual acoustophoretic chamber |
| GB201503578D0 (en) * | 2015-03-03 | 2015-04-15 | Ge Healthcare Bio Sciences Ab | Sanitization method for affinity chromatography matrices |
| US11021699B2 (en) | 2015-04-29 | 2021-06-01 | FioDesign Sonics, Inc. | Separation using angled acoustic waves |
| US11708572B2 (en) | 2015-04-29 | 2023-07-25 | Flodesign Sonics, Inc. | Acoustic cell separation techniques and processes |
| US11377651B2 (en) | 2016-10-19 | 2022-07-05 | Flodesign Sonics, Inc. | Cell therapy processes utilizing acoustophoresis |
| EP3015542A1 (de) * | 2015-05-07 | 2016-05-04 | Bayer Technology Services GmbH | Modulare anlage und verfahren zur kontinuierlichen, keimreduzierten produktion und/oder aufbereitung eines produktes |
| US11459540B2 (en) | 2015-07-28 | 2022-10-04 | Flodesign Sonics, Inc. | Expanded bed affinity selection |
| US11474085B2 (en) | 2015-07-28 | 2022-10-18 | Flodesign Sonics, Inc. | Expanded bed affinity selection |
| US20170101437A1 (en) * | 2015-10-09 | 2017-04-13 | Hetero Drugs Ltd. | Process for purification of darbepoetin alfa |
| US11214789B2 (en) | 2016-05-03 | 2022-01-04 | Flodesign Sonics, Inc. | Concentration and washing of particles with acoustics |
| US11085035B2 (en) | 2016-05-03 | 2021-08-10 | Flodesign Sonics, Inc. | Therapeutic cell washing, concentration, and separation utilizing acoustophoresis |
| US20190211055A1 (en) * | 2016-09-14 | 2019-07-11 | Kinbio Ltd. | Methods of purifying and qualifying antibodies |
| CN110494543A (zh) | 2016-10-19 | 2019-11-22 | 弗洛设计声能学公司 | 通过声学的亲和细胞提取 |
| US11697672B2 (en) * | 2017-03-24 | 2023-07-11 | Council Of Scientific & Industrial Research | Process for the purification of recombinant antibody fragments |
| GB201711481D0 (en) * | 2017-07-17 | 2017-08-30 | Ucb Biopharma Sprl | Protein purification |
| JP6957738B2 (ja) * | 2017-08-31 | 2021-11-02 | グリーン・クロス・コーポレイションＧｒｅｅｎ Ｃｒｏｓｓ Ｃｏｒｐ． | スルファターゼタンパク質を精製する方法 |
| JP2021507561A (ja) | 2017-12-14 | 2021-02-22 | フロデザイン ソニックス， インク．Ｆｌｏｄｅｓｉｇｎ Ｓｏｎｉｃｓ， Ｉｎｃ． | 音響トランスデューサドライバ及びコントローラ |
| CN119881293A (zh) | 2018-03-21 | 2025-04-25 | 沃特世科技公司 | 基于非抗体高亲和力的样品制备、吸附剂、装置和方法 |
| EP3546475A1 (en) | 2018-03-27 | 2019-10-02 | Sanofi | Full flow-through process for purifying recombinant proteins |
| US12071607B2 (en) * | 2018-06-01 | 2024-08-27 | Lonza Ltd. | Midscale model for organic growth and phasing |
| KR102337683B1 (ko) | 2018-09-21 | 2021-12-13 | 주식회사 녹십자 | 고효율 항-tfpi 항체 조성물 |
| EP3636657A1 (en) | 2018-10-08 | 2020-04-15 | Ablynx N.V. | Chromatography-free antibody purification method |
| WO2020084503A1 (en) * | 2018-10-26 | 2020-04-30 | Cadila Healthcare Limited | A composition comprising antibody with reduced level of basic variants thereof |
| WO2020183332A1 (en) * | 2019-03-11 | 2020-09-17 | Intas Pharmaceuticals Ltd. | Purification of adalimumab using tandem chromatography |
| CA3135611A1 (en) * | 2019-04-03 | 2020-10-08 | Genzyme Corporation | Continuous production of recombinant proteins |
| CN114026108B (zh) * | 2019-06-28 | 2024-09-10 | 夏尔巴生物技术(苏州)有限公司 | 无缝连续流层析方法 |
| EP4034546A4 (en) * | 2019-09-23 | 2024-01-31 | Merck Sharp & Dohme LLC | METHODS AND COMPOSITIONS COMPRISING AN ANTI-CTLA4 MONOCLONAL ANTIBODY WITH REDUCED HOST CELL PROTEINS AND INCREASED POLYSORBATE 80 STABILITY |
| KR102154952B1 (ko) * | 2020-02-21 | 2020-09-10 | 프레스티지바이오로직스 주식회사 | 아달리무맙의 Non-Protein A 정제방법 |
| CN112574321B (zh) * | 2020-12-30 | 2023-10-20 | 上海赛金生物医药有限公司 | 一种捕获单克隆抗体-肿瘤坏死因子融合蛋白的亲和纯化方法 |
| WO2022234412A1 (en) | 2021-05-03 | 2022-11-10 | Lupin Limited | A process for purification of fc-fusion proteins |
Family Cites Families (34)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| KR930008447B1 (ko) | 1987-10-23 | 1993-09-04 | 쉐링 코포레이션 | 단백질 정제방법 |
| UA35599C2 (uk) * | 1993-09-21 | 2001-04-16 | Хемосол Інк | Спосіб очищення гемоглобіну з сирого розчину |
| CA2106612C (en) | 1993-09-21 | 2001-02-06 | Diana Pliura | Displacement chromatography process |
| US5891741A (en) | 1997-05-16 | 1999-04-06 | Coulter International Corp. | Antibody-aminodextran-phycobiliprotein conjugates |
| CN1136317C (zh) | 1999-03-12 | 2004-01-28 | 中国人民解放军第四军医大学 | 单克隆抗体双段和单段的制备方法 |
| US20020009445A1 (en) | 2000-07-12 | 2002-01-24 | Yansheng Du | Human beta-amyloid antibody and use thereof for treatment of alzheimer's disease |
| US6602855B2 (en) | 2001-04-30 | 2003-08-05 | Syn X Pharma, Inc. | Biopolymer marker indicative of disease state having a molecular weight of 1449 daltons |
| CN1504482A (zh) | 2002-12-03 | 2004-06-16 | 北京优力凯生物技术有限责任公司 | 无细胞百日咳抗原蛋白的分离纯化方法 |
| PT1745075E (pt) | 2004-04-21 | 2013-06-17 | Brigham & Womens Hospital | Péptidos de ligação a poli-n-acetilglucosamina (pnag/dpnag) e métodos da sua utilização |
| EP1807205B1 (en) * | 2004-10-21 | 2012-09-26 | GE Healthcare Bio-Sciences AB | A method of antibody purification |
| CA2602375C (en) | 2005-03-23 | 2018-07-24 | Genmab A/S | Antibodies against cd38 for treatment of multiple myeloma |
| CN1814775A (zh) | 2005-12-06 | 2006-08-09 | 中国海洋大学 | 一种抗病毒活性寡聚肽的制备方法 |
| EP1914242A1 (en) * | 2006-10-19 | 2008-04-23 | Sanofi-Aventis | Novel anti-CD38 antibodies for the treatment of cancer |
| AU2008274195B2 (en) * | 2007-07-11 | 2013-09-05 | Novo Nordisk A/S | Purification of factor VIII using a mixed-mode or multimodal resin |
| MY158903A (en) | 2007-11-16 | 2016-11-30 | Univ Rockefeller | Antibodies specific for the protofibril form of beta-amyloid protein |
| TWI472339B (zh) * | 2008-01-30 | 2015-02-11 | Genentech Inc | 包含結合至ｈｅｒ２結構域ii之抗體及其酸性變異體的組合物 |
| EP2260054B1 (en) * | 2008-02-29 | 2015-06-03 | Biogen Idec MA Inc. | Purified immunoglobulin fusion proteins and methods of their purification |
| EP2281000A2 (en) | 2008-05-15 | 2011-02-09 | Novo Nordisk A/S | Antibody purification process |
| WO2010009388A1 (en) * | 2008-07-18 | 2010-01-21 | Talecris Biotherapeutics, Inc. | Method of preparing alpha-1 proteinase inhibitor |
| EP2360183B1 (en) | 2008-12-19 | 2016-07-27 | Takeda Pharmaceutical Company Limited | Antibody purification method by mixed mode chromatography utilizing an arginine-containing loading solution |
| CN102272146A (zh) | 2009-01-13 | 2011-12-07 | 通用电气健康护理生物科学股份公司 | 用带负电的聚合物沉淀生物分子 |
| KR101224468B1 (ko) * | 2009-05-20 | 2013-01-23 | 주식회사 파멥신 | 신규한 형태의 이중표적항체 및 그 용도 |
| KR101415660B1 (ko) * | 2009-08-07 | 2014-07-16 | 이엠디 밀리포어 코포레이션 | 샘플 중의 1 이상의 불순물로부터 표적 단백질을 정제하는 방법 |
| US9527010B2 (en) * | 2009-09-25 | 2016-12-27 | Ge Healthcare Bio-Sciences Corp. | Separation system and method |
| US20120208986A1 (en) * | 2009-10-20 | 2012-08-16 | Wenger Marc D | Use of mixed mode chromatography for the capture and purification of basic antibody products |
| WO2011090719A2 (en) | 2009-12-29 | 2011-07-28 | Dr. Reddy's Laboratories Ltd. | Protein purification by ion exchange |
| EP2415779B1 (en) | 2010-08-02 | 2015-01-21 | ratiopharm GmbH | Method of producing and purifying an active soluble sialyltransferase |
| WO2012125735A1 (en) * | 2011-03-15 | 2012-09-20 | Abott Laboratories | An integrated approach to the isolation and purification of antibodies |
| CA2831787A1 (en) | 2011-03-29 | 2012-10-04 | Glaxosmithkline Llc | Buffer system for protein purification |
| ES2915263T3 (es) | 2011-06-17 | 2022-06-21 | Roche Diagnostics Hematology Inc | Solución y procedimiento para el histoprocesamiento de muestras biológicas |
| WO2013028330A2 (en) | 2011-08-19 | 2013-02-28 | Emd Millipore Corporation | Methods of reducing level of one of more impurities in a sample during protein purification |
| EP2578286A1 (en) * | 2011-10-04 | 2013-04-10 | Merck Patent GmbH | Method and apparatus for chromatographic purification |
| JP6431372B2 (ja) * | 2011-10-25 | 2018-11-28 | プロシーナ バイオサイエンシーズ リミテッド | 抗体製剤および方法 |
| WO2013075740A1 (en) * | 2011-11-23 | 2013-05-30 | Sanofi | Antibody purification method |
-
2014
- 2014-05-06 EP EP14722194.9A patent/EP2994485B1/en active Active
- 2014-05-06 US US14/889,397 patent/US10793622B2/en active Active
- 2014-05-06 HU HUE17200909A patent/HUE057119T2/hu unknown
- 2014-05-06 TW TW103116153A patent/TWI631132B/zh not_active IP Right Cessation
- 2014-05-06 SG SG11201508968XA patent/SG11201508968XA/en unknown
- 2014-05-06 ES ES17200909T patent/ES2905675T3/es active Active
- 2014-05-06 CN CN201480038360.9A patent/CN105358572A/zh active Pending
- 2014-05-06 ES ES14722194.9T patent/ES2665645T3/es active Active
- 2014-05-06 DK DK14722194.9T patent/DK2994485T3/en active
- 2014-05-06 WO PCT/EP2014/059246 patent/WO2014180852A1/en not_active Ceased
- 2014-05-06 AU AU2014264697A patent/AU2014264697B2/en active Active
- 2014-05-06 CA CA2911462A patent/CA2911462C/en active Active
- 2014-05-06 RU RU2015151869A patent/RU2662668C2/ru active
- 2014-05-06 HU HUE14722194A patent/HUE038741T2/hu unknown
- 2014-05-06 DK DK17200909.4T patent/DK3301115T3/da active
- 2014-05-06 KR KR1020157032904A patent/KR102272851B1/ko active Active
- 2014-05-06 NO NO14722194A patent/NO2994485T3/no unknown
- 2014-05-06 TW TW107117528A patent/TWI675041B/zh not_active IP Right Cessation
- 2014-05-06 MX MX2015015482A patent/MX368177B/es active IP Right Grant
- 2014-05-06 BR BR112015027812-4A patent/BR112015027812B1/pt active IP Right Grant
- 2014-05-06 JP JP2016512344A patent/JP6463734B2/ja active Active
- 2014-05-06 EP EP17200909.4A patent/EP3301115B1/en active Active
- 2014-05-06 CN CN202310118200.6A patent/CN116003579A/zh active Pending
-
2015
- 2015-11-02 IL IL242408A patent/IL242408B/en active IP Right Grant
-
2019
- 2019-01-10 JP JP2019002288A patent/JP2019104735A/ja active Pending
-
2022
- 2022-02-09 CY CY20221100113T patent/CY1125281T1/el unknown
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| DK2994485T3 (en) | CONTINUOUS MULTIPLE STEP PROCEDURE FOR PURIFICATION OF ANTIBODIES | |
| AU2017245478B2 (en) | Protein purification using Bis-Tris buffer | |
| AU2019246328B2 (en) | Full flow-through process for purifying recombinant proteins | |
| EP2782925B1 (en) | Protein purification using bis-tris buffer |