ES2534936T3 - Método para producir y purificar una sialiltransferasa soluble activa - Google Patents
Método para producir y purificar una sialiltransferasa soluble activa Download PDFInfo
- Publication number
- ES2534936T3 ES2534936T3 ES10171626.4T ES10171626T ES2534936T3 ES 2534936 T3 ES2534936 T3 ES 2534936T3 ES 10171626 T ES10171626 T ES 10171626T ES 2534936 T3 ES2534936 T3 ES 2534936T3
- Authority
- ES
- Spain
- Prior art keywords
- sialyltransferase
- st6galnaci
- chromatography
- column
- stage
- 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.)
- Active
Links
- 108090000141 Sialyltransferases Proteins 0.000 title abstract description 23
- 102000003838 Sialyltransferases Human genes 0.000 title abstract description 23
- 238000004519 manufacturing process Methods 0.000 title description 6
- 108010070543 CMP-N-acetylneuraminate-alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase Proteins 0.000 abstract description 31
- 102100031969 Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 1 Human genes 0.000 abstract description 23
- 102000004196 processed proteins & peptides Human genes 0.000 abstract description 22
- 108090000765 processed proteins & peptides Proteins 0.000 abstract description 22
- 229920001184 polypeptide Polymers 0.000 abstract description 21
- 238000000034 method Methods 0.000 abstract description 17
- 238000005277 cation exchange chromatography Methods 0.000 abstract description 13
- 238000001042 affinity chromatography Methods 0.000 abstract description 11
- 238000005571 anion exchange chromatography Methods 0.000 abstract description 10
- 238000012434 mixed-mode chromatography Methods 0.000 abstract description 4
- 210000004978 chinese hamster ovary cell Anatomy 0.000 abstract description 2
- 239000006143 cell culture medium Substances 0.000 abstract 3
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 31
- 239000011780 sodium chloride Substances 0.000 description 16
- 229920002684 Sepharose Polymers 0.000 description 14
- 239000000872 buffer Substances 0.000 description 13
- 230000000694 effects Effects 0.000 description 13
- 239000011347 resin Substances 0.000 description 12
- 229920005989 resin Polymers 0.000 description 12
- 238000000108 ultra-filtration Methods 0.000 description 9
- 239000012564 Q sepharose fast flow resin Substances 0.000 description 8
- 238000004007 reversed phase HPLC Methods 0.000 description 8
- LWIHDJKSTIGBAC-UHFFFAOYSA-K tripotassium phosphate Chemical compound [K+].[K+].[K+].[O-]P([O-])([O-])=O LWIHDJKSTIGBAC-UHFFFAOYSA-K 0.000 description 8
- 238000011026 diafiltration Methods 0.000 description 7
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- 102000004169 proteins and genes Human genes 0.000 description 7
- 108090000623 proteins and genes Proteins 0.000 description 7
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- OWMVSZAMULFTJU-UHFFFAOYSA-N bis-tris Chemical compound OCCN(CCO)C(CO)(CO)CO OWMVSZAMULFTJU-UHFFFAOYSA-N 0.000 description 5
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- 208000001020 chondrodysplasia punctata Diseases 0.000 description 5
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- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 5
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- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 4
- 230000001225 therapeutic effect Effects 0.000 description 4
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 3
- FBPFZTCFMRRESA-FSIIMWSLSA-N D-Glucitol Natural products OC[C@H](O)[C@H](O)[C@@H](O)[C@H](O)CO FBPFZTCFMRRESA-FSIIMWSLSA-N 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- OFOBLEOULBTSOW-UHFFFAOYSA-N Propanedioic acid Natural products OC(=O)CC(O)=O OFOBLEOULBTSOW-UHFFFAOYSA-N 0.000 description 3
- 238000010521 absorption reaction Methods 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
- 230000013595 glycosylation Effects 0.000 description 3
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- 235000010482 polyoxyethylene sorbitan monooleate Nutrition 0.000 description 3
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- 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 2
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 2
- 108090000394 Erythropoietin Proteins 0.000 description 2
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- 125000000524 functional group Chemical group 0.000 description 2
- 125000003147 glycosyl group Chemical group 0.000 description 2
- 150000002500 ions Chemical class 0.000 description 2
- JVTAAEKCZFNVCJ-UHFFFAOYSA-N lactic acid Chemical compound CC(O)C(O)=O JVTAAEKCZFNVCJ-UHFFFAOYSA-N 0.000 description 2
- BDAGIHXWWSANSR-UHFFFAOYSA-N methanoic acid Natural products OC=O BDAGIHXWWSANSR-UHFFFAOYSA-N 0.000 description 2
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- 238000012360 testing method Methods 0.000 description 2
- 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 description 1
- KWTQSFXGGICVPE-UHFFFAOYSA-N 2-amino-5-(diaminomethylideneamino)pentanoic acid;hydron;chloride Chemical compound Cl.OC(=O)C(N)CCCN=C(N)N KWTQSFXGGICVPE-UHFFFAOYSA-N 0.000 description 1
- OSWFIVFLDKOXQC-UHFFFAOYSA-N 4-(3-methoxyphenyl)aniline Chemical compound COC1=CC=CC(C=2C=CC(N)=CC=2)=C1 OSWFIVFLDKOXQC-UHFFFAOYSA-N 0.000 description 1
- 229920000936 Agarose Polymers 0.000 description 1
- KWTQSFXGGICVPE-WCCKRBBISA-N Arginine hydrochloride Chemical compound Cl.OC(=O)[C@@H](N)CCCN=C(N)N KWTQSFXGGICVPE-WCCKRBBISA-N 0.000 description 1
- LSNNMFCWUKXFEE-UHFFFAOYSA-M Bisulfite Chemical compound OS([O-])=O LSNNMFCWUKXFEE-UHFFFAOYSA-M 0.000 description 1
- TXCIAUNLDRJGJZ-UHFFFAOYSA-N CMP-N-acetyl neuraminic acid Natural products O1C(C(O)C(O)CO)C(NC(=O)C)C(O)CC1(C(O)=O)OP(O)(=O)OCC1C(O)C(O)C(N2C(N=C(N)C=C2)=O)O1 TXCIAUNLDRJGJZ-UHFFFAOYSA-N 0.000 description 1
- TXCIAUNLDRJGJZ-BILDWYJOSA-N CMP-N-acetyl-beta-neuraminic acid Chemical compound O1[C@@H]([C@H](O)[C@H](O)CO)[C@H](NC(=O)C)[C@@H](O)C[C@]1(C(O)=O)OP(O)(=O)OC[C@@H]1[C@@H](O)[C@@H](O)[C@H](N2C(N=C(N)C=C2)=O)O1 TXCIAUNLDRJGJZ-BILDWYJOSA-N 0.000 description 1
- 102000003951 Erythropoietin Human genes 0.000 description 1
- 241000287828 Gallus gallus Species 0.000 description 1
- 102000002068 Glycopeptides Human genes 0.000 description 1
- 108010015899 Glycopeptides Proteins 0.000 description 1
- 102000003886 Glycoproteins Human genes 0.000 description 1
- 108090000288 Glycoproteins Proteins 0.000 description 1
- 102000051366 Glycosyltransferases Human genes 0.000 description 1
- 108700023372 Glycosyltransferases Proteins 0.000 description 1
- 108010017080 Granulocyte Colony-Stimulating Factor Proteins 0.000 description 1
- 102000004269 Granulocyte Colony-Stimulating Factor Human genes 0.000 description 1
- 239000007995 HEPES buffer Substances 0.000 description 1
- 101000976075 Homo sapiens Insulin Proteins 0.000 description 1
- 101000959820 Homo sapiens Interferon alpha-1/13 Proteins 0.000 description 1
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- FSVCELGFZIQNCK-UHFFFAOYSA-N N,N-bis(2-hydroxyethyl)glycine Chemical compound OCCN(CCO)CC(O)=O FSVCELGFZIQNCK-UHFFFAOYSA-N 0.000 description 1
- OVRNDRQMDRJTHS-KEWYIRBNSA-N N-acetyl-D-galactosamine Chemical compound CC(=O)N[C@H]1C(O)O[C@H](CO)[C@H](O)[C@@H]1O OVRNDRQMDRJTHS-KEWYIRBNSA-N 0.000 description 1
- MBLBDJOUHNCFQT-UHFFFAOYSA-N N-acetyl-D-galactosamine Natural products CC(=O)NC(C=O)C(O)C(O)C(O)CO MBLBDJOUHNCFQT-UHFFFAOYSA-N 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 239000002202 Polyethylene glycol Substances 0.000 description 1
- 239000012614 Q-Sepharose Substances 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 1
- 239000004473 Threonine Substances 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- VJHCJDRQFCCTHL-UHFFFAOYSA-N acetic acid 2,3,4,5,6-pentahydroxyhexanal Chemical compound CC(O)=O.OCC(O)C(O)C(O)C(O)C=O VJHCJDRQFCCTHL-UHFFFAOYSA-N 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 125000000217 alkyl group Chemical group 0.000 description 1
- 150000001413 amino acids Chemical group 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
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- 229960003589 arginine hydrochloride Drugs 0.000 description 1
- 239000011324 bead Substances 0.000 description 1
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- 125000002057 carboxymethyl group Chemical group [H]OC(=O)C([H])([H])[*] 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
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- YKCWQPZFAFZLBI-UHFFFAOYSA-N cibacron blue Chemical group C1=2C(=O)C3=CC=CC=C3C(=O)C=2C(N)=C(S(O)(=O)=O)C=C1NC(C=C1S(O)(=O)=O)=CC=C1NC(N=1)=NC(Cl)=NC=1NC1=CC=CC=C1S(O)(=O)=O YKCWQPZFAFZLBI-UHFFFAOYSA-N 0.000 description 1
- 235000015165 citric acid Nutrition 0.000 description 1
- 230000000052 comparative effect Effects 0.000 description 1
- 238000003271 compound fluorescence assay Methods 0.000 description 1
- 230000021615 conjugation Effects 0.000 description 1
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- 239000003480 eluent Substances 0.000 description 1
- 238000010828 elution Methods 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 229940105423 erythropoietin Drugs 0.000 description 1
- 230000007717 exclusion Effects 0.000 description 1
- 239000012530 fluid Substances 0.000 description 1
- 235000019253 formic acid Nutrition 0.000 description 1
- 238000009472 formulation Methods 0.000 description 1
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- PBGKTOXHQIOBKM-FHFVDXKLSA-N insulin (human) Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@H]1CSSC[C@H]2C(=O)N[C@H](C(=O)N[C@@H](CO)C(=O)N[C@H](C(=O)N[C@H](C(N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=3C=CC(O)=CC=3)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=3NC=NC=3)NC(=O)[C@H](CO)NC(=O)CNC1=O)C(=O)NCC(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)NCC(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H]([C@@H](C)O)C(O)=O)C(=O)N[C@@H](CC(N)=O)C(O)=O)=O)CSSC[C@@H](C(N2)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@@H](NC(=O)CN)[C@@H](C)CC)[C@@H](C)CC)[C@@H](C)O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](NC(=O)[C@@H](N)CC=1C=CC=CC=1)C(C)C)C1=CN=CN1 PBGKTOXHQIOBKM-FHFVDXKLSA-N 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 239000004310 lactic acid Substances 0.000 description 1
- 235000014655 lactic acid Nutrition 0.000 description 1
- 239000003446 ligand Substances 0.000 description 1
- 239000007788 liquid Substances 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
- 239000011976 maleic acid Substances 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 238000005374 membrane filtration Methods 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- XYJRXVWERLGGKC-UHFFFAOYSA-D pentacalcium;hydroxide;triphosphate Chemical compound [OH-].[Ca+2].[Ca+2].[Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O XYJRXVWERLGGKC-UHFFFAOYSA-D 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 229920001467 poly(styrenesulfonates) Polymers 0.000 description 1
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
- 239000011148 porous material Substances 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
- 239000012460 protein solution Substances 0.000 description 1
- 230000002285 radioactive effect Effects 0.000 description 1
- 238000012827 research and development Methods 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 239000012723 sample buffer Substances 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 229910052709 silver Inorganic materials 0.000 description 1
- 239000004332 silver Substances 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 238000012799 strong cation exchange Methods 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 150000003467 sulfuric acid derivatives Chemical class 0.000 description 1
- 238000010998 test method Methods 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
- 238000012546 transfer Methods 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/10—Transferases (2.)
- C12N9/1048—Glycosyltransferases (2.4)
- C12N9/1081—Glycosyltransferases (2.4) transferring other glycosyl groups (2.4.99)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y204/00—Glycosyltransferases (2.4)
- C12Y204/99—Glycosyltransferases (2.4) transferring other glycosyl groups (2.4.99)
- C12Y204/99003—Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase (2.4.99.3)
Landscapes
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Wood Science & Technology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Genetics & Genomics (AREA)
- Engineering & Computer Science (AREA)
- Zoology (AREA)
- General Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Molecular Biology (AREA)
- Medicinal Chemistry (AREA)
- Biomedical Technology (AREA)
- Biotechnology (AREA)
- Microbiology (AREA)
- Enzymes And Modification Thereof (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
- Medicinal Preparation (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP20100171626 EP2415779B1 (en) | 2010-08-02 | 2010-08-02 | Method of producing and purifying an active soluble sialyltransferase |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| ES2534936T3 true ES2534936T3 (es) | 2015-04-30 |
Family
ID=42736163
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| ES10171626.4T Active ES2534936T3 (es) | 2010-08-02 | 2010-08-02 | Método para producir y purificar una sialiltransferasa soluble activa |
Country Status (9)
| Country | Link |
|---|---|
| US (1) | US9222081B2 (OSRAM) |
| EP (2) | EP2415779B1 (OSRAM) |
| JP (1) | JP5984267B2 (OSRAM) |
| CN (1) | CN103154017B (OSRAM) |
| CA (1) | CA2807397C (OSRAM) |
| ES (1) | ES2534936T3 (OSRAM) |
| MX (1) | MX2013001447A (OSRAM) |
| PT (1) | PT2415779E (OSRAM) |
| WO (1) | WO2012016984A1 (OSRAM) |
Families Citing this family (15)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2013075740A1 (en) | 2011-11-23 | 2013-05-30 | Sanofi | Antibody purification method |
| JP2016513245A (ja) * | 2013-02-06 | 2016-05-12 | エイジェンシー・フォー・サイエンス，テクノロジー・アンド・リサーチ | タンパク質製剤の凝集体含有量を減少させる混合多官能金属親和性表面 |
| HUE038741T2 (hu) | 2013-05-06 | 2018-11-28 | Sanofi Sa | Folyamatos többlépéses eljárás antitestek tisztítására |
| KR20170132293A (ko) * | 2015-03-31 | 2017-12-01 | 예다 리서치 앤드 디벨럽먼트 캄파니 리미티드 | 글루타메이트 옥살로아세테이트 트랜스아미나제 1（ｇｏｔ１） 제제와 이의 제조방법 및 용도 |
| KR101667677B1 (ko) * | 2015-05-29 | 2016-10-19 | 한국생명공학연구원 | 재조합 ST6Gal1 단백질을 활성형으로 제조하는 방법 |
| EP3559250A1 (en) | 2016-12-21 | 2019-10-30 | H. Hoffnabb-La Roche Ag | Re-use of enzymes in in vitro glycoengineering of antibodies |
| AU2017381657B2 (en) | 2016-12-21 | 2020-07-23 | F. Hoffmann-La Roche Ag | Method for in vitro glycoengineering of antibodies |
| EP3678687B1 (en) | 2017-09-04 | 2022-08-17 | 89Bio Ltd. | Mutant fgf-21 peptide conjugates and uses thereof |
| WO2019063849A1 (en) * | 2017-12-20 | 2019-04-04 | Dsm Ip Assets B.V. | PURIFICATION OF A POLYPEPTIDE OF INTEREST |
| EP3546475A1 (en) | 2018-03-27 | 2019-10-02 | Sanofi | Full flow-through process for purifying recombinant proteins |
| KR102362777B1 (ko) * | 2018-03-27 | 2022-02-15 | 주식회사 녹십자 | 친화성 크로마토그래피 공정을 포함하는 백일해균 유래 단백질 수득 방법 |
| KR102140531B1 (ko) * | 2018-08-07 | 2020-08-04 | (주)휴온스 | Gly-Tβ4의 제조방법 |
| EP3613486B1 (de) * | 2018-08-24 | 2020-10-07 | UGA Biopharma GmbH | Verfahren und anlage zur reinigung von epo und/oder einem epo-derivat |
| CN113416243B (zh) * | 2021-08-23 | 2021-12-10 | 上海盛迪医药有限公司 | 一种纯化抗体的方法 |
| CN119912505A (zh) * | 2025-04-02 | 2025-05-02 | 浙江熙正霖生物科技有限公司 | 一种从发酵液中提纯唾液酸的方法 |
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| US5032519A (en) * | 1989-10-24 | 1991-07-16 | The Regents Of The Univ. Of California | Method for producing secretable glycosyltransferases and other Golgi processing enzymes |
| EP0737745A4 (en) | 1993-12-24 | 1999-06-16 | Rikagaku Kenkyusho | INNOVATIVE SYNTHETASE FOR SUGAR CHAINS AND METHOD FOR THEIR PRODUCTION |
| US6280989B1 (en) * | 1999-06-17 | 2001-08-28 | Dmitri Kapitonov | Sialyltransferases |
| ES2561985T3 (es) | 2001-10-10 | 2016-03-01 | Ratiopharm Gmbh | Remodelación y glicoconjugación de anticuerpos |
| CN1897812B (zh) * | 2003-12-03 | 2011-08-17 | 生物种属学股份公司 | 糖聚乙二醇化的粒细胞集落刺激因子 |
| WO2005121332A2 (en) | 2004-06-03 | 2005-12-22 | Neose Technologies, Inc. | Truncated st6galnaci polypeptides and nucleic acids |
| KR20080021590A (ko) | 2005-03-24 | 2008-03-07 | 네오스 테크놀로지스, 인크. | 가용성이고 활성인 진핵생물 글리코실트랜스퍼라제의원핵생물 유기체 내에서의 발현 |
| US20060246544A1 (en) | 2005-03-30 | 2006-11-02 | Neose Technologies,Inc. | Manufacturing process for the production of peptides grown in insect cell lines |
| WO2007056524A2 (en) | 2005-11-09 | 2007-05-18 | Neose Technologies, Inc. | St3gal-1/st6galnac-1 chimeras |
| JP2010505874A (ja) * | 2006-10-03 | 2010-02-25 | ノヴォ ノルディスク アー／エス | ポリペプチドコンジュゲートの精製方法 |
| US20080207487A1 (en) | 2006-11-02 | 2008-08-28 | Neose Technologies, Inc. | Manufacturing process for the production of polypeptides expressed in insect cell-lines |
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| EP2415779B1 (en) | 2015-01-21 |
| CN103154017A (zh) | 2013-06-12 |
| PT2415779E (pt) | 2015-05-13 |
| US9222081B2 (en) | 2015-12-29 |
| EP2601207A1 (en) | 2013-06-12 |
| JP5984267B2 (ja) | 2016-09-06 |
| EP2601207B1 (en) | 2016-12-28 |
| CN103154017B (zh) | 2016-02-03 |
| CA2807397C (en) | 2019-03-19 |
| JP2013535207A (ja) | 2013-09-12 |
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