OA10753A - Process for controlling sialylation of proteins produced by mammalian cell culture - Google Patents
Process for controlling sialylation of proteins produced by mammalian cell culture Download PDFInfo
- Publication number
- OA10753A OA10753A OA70153A OA70153A OA10753A OA 10753 A OA10753 A OA 10753A OA 70153 A OA70153 A OA 70153A OA 70153 A OA70153 A OA 70153A OA 10753 A OA10753 A OA 10753A
- Authority
- OA
- OAPI
- Prior art keywords
- cell
- igg
- tnfrl
- cell culture
- culture
- Prior art date
Links
- 238000000034 method Methods 0.000 title claims abstract description 107
- 238000004113 cell culture Methods 0.000 title claims abstract description 83
- 230000008569 process Effects 0.000 title claims abstract description 73
- 210000004962 mammalian cell Anatomy 0.000 title claims abstract description 20
- 108090000623 proteins and genes Proteins 0.000 title claims description 60
- 102000004169 proteins and genes Human genes 0.000 title claims description 54
- 230000009450 sialylation Effects 0.000 title description 9
- 210000004027 cell Anatomy 0.000 claims abstract description 170
- SQVRNKJHWKZAKO-UHFFFAOYSA-N beta-N-Acetyl-D-neuraminic acid Natural products CC(=O)NC1C(O)CC(O)(C(O)=O)OC1C(O)C(O)CO SQVRNKJHWKZAKO-UHFFFAOYSA-N 0.000 claims abstract description 76
- SQVRNKJHWKZAKO-OQPLDHBCSA-N sialic acid Chemical compound CC(=O)N[C@@H]1[C@@H](O)C[C@@](O)(C(O)=O)OC1[C@H](O)[C@H](O)CO SQVRNKJHWKZAKO-OQPLDHBCSA-N 0.000 claims abstract description 75
- 238000004519 manufacturing process Methods 0.000 claims abstract description 66
- 102000003886 Glycoproteins Human genes 0.000 claims abstract description 46
- 108090000288 Glycoproteins Proteins 0.000 claims abstract description 46
- 108060008682 Tumor Necrosis Factor Proteins 0.000 claims abstract description 11
- 239000002253 acid Substances 0.000 claims description 41
- 239000000203 mixture Substances 0.000 claims description 23
- 150000002482 oligosaccharides Chemical class 0.000 claims description 18
- MFBOGIVSZKQAPD-UHFFFAOYSA-M sodium butyrate Chemical compound [Na+].CCCC([O-])=O MFBOGIVSZKQAPD-UHFFFAOYSA-M 0.000 claims description 15
- OVRNDRQMDRJTHS-UHFFFAOYSA-N N-acelyl-D-glucosamine Natural products CC(=O)NC1C(O)OC(CO)C(O)C1O OVRNDRQMDRJTHS-UHFFFAOYSA-N 0.000 claims description 13
- MBLBDJOUHNCFQT-LXGUWJNJSA-N N-acetylglucosamine Natural products CC(=O)N[C@@H](C=O)[C@@H](O)[C@H](O)[C@H](O)CO MBLBDJOUHNCFQT-LXGUWJNJSA-N 0.000 claims description 13
- 230000003698 anagen phase Effects 0.000 claims description 13
- 210000004978 chinese hamster ovary cell Anatomy 0.000 claims description 13
- 229920001542 oligosaccharide Polymers 0.000 claims description 12
- 239000011734 sodium Substances 0.000 claims description 11
- 238000012258 culturing Methods 0.000 claims description 10
- OVRNDRQMDRJTHS-FMDGEEDCSA-N N-acetyl-beta-D-glucosamine Chemical group 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 9
- 230000003247 decreasing effect Effects 0.000 claims description 9
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 claims description 8
- 229910052708 sodium Inorganic materials 0.000 claims description 8
- 239000002299 complementary DNA Substances 0.000 claims description 6
- 229950006780 n-acetylglucosamine Drugs 0.000 claims description 6
- 230000001225 therapeutic effect Effects 0.000 claims description 6
- 108060008683 Tumor Necrosis Factor Receptor Proteins 0.000 claims description 5
- 101710187743 Tumor necrosis factor receptor superfamily member 1A Proteins 0.000 claims description 5
- 102100033732 Tumor necrosis factor receptor superfamily member 1A Human genes 0.000 claims description 5
- 102000003298 tumor necrosis factor receptor Human genes 0.000 claims description 5
- 229940027941 immunoglobulin g Drugs 0.000 claims description 3
- 239000013598 vector Substances 0.000 claims description 3
- 239000000546 pharmaceutical excipient Substances 0.000 claims description 2
- SGPGESCZOCHFCL-UHFFFAOYSA-N Tilisolol hydrochloride Chemical compound [Cl-].C1=CC=C2C(=O)N(C)C=C(OCC(O)C[NH2+]C(C)(C)C)C2=C1 SGPGESCZOCHFCL-UHFFFAOYSA-N 0.000 claims 8
- 102000003390 tumor necrosis factor Human genes 0.000 claims 6
- MSWZFWKMSRAUBD-IVMDWMLBSA-N 2-amino-2-deoxy-D-glucopyranose Chemical compound N[C@H]1C(O)O[C@H](CO)[C@@H](O)[C@@H]1O MSWZFWKMSRAUBD-IVMDWMLBSA-N 0.000 claims 1
- MSWZFWKMSRAUBD-UHFFFAOYSA-N beta-D-galactosamine Natural products NC1C(O)OC(CO)C(O)C1O MSWZFWKMSRAUBD-UHFFFAOYSA-N 0.000 claims 1
- OEYIOHPDSNJKLS-UHFFFAOYSA-N choline Chemical compound C[N+](C)(C)CCO OEYIOHPDSNJKLS-UHFFFAOYSA-N 0.000 claims 1
- 229960001231 choline Drugs 0.000 claims 1
- 229960002442 glucosamine Drugs 0.000 claims 1
- 238000013518 transcription Methods 0.000 abstract description 13
- 230000035897 transcription Effects 0.000 abstract description 13
- 239000003623 enhancer Substances 0.000 abstract description 9
- 102000000852 Tumor Necrosis Factor-alpha Human genes 0.000 abstract description 5
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 abstract description 5
- 208000035475 disorder Diseases 0.000 abstract description 3
- 238000002360 preparation method Methods 0.000 abstract description 3
- 230000002757 inflammatory effect Effects 0.000 abstract description 2
- 108060003951 Immunoglobulin Proteins 0.000 abstract 1
- 102000018358 immunoglobulin Human genes 0.000 abstract 1
- 235000018102 proteins Nutrition 0.000 description 49
- 235000014633 carbohydrates Nutrition 0.000 description 22
- 239000001963 growth medium Substances 0.000 description 22
- 239000002609 medium Substances 0.000 description 22
- 150000001720 carbohydrates Chemical class 0.000 description 21
- 239000000047 product Substances 0.000 description 20
- 108090000765 processed proteins & peptides Proteins 0.000 description 16
- 230000012010 growth Effects 0.000 description 15
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 12
- IQFYYKKMVGJFEH-XLPZGREQSA-N Thymidine Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](CO)[C@@H](O)C1 IQFYYKKMVGJFEH-XLPZGREQSA-N 0.000 description 12
- 102000004196 processed proteins & peptides Human genes 0.000 description 12
- 102000005962 receptors Human genes 0.000 description 12
- 108020003175 receptors Proteins 0.000 description 12
- FERIUCNNQQJTOY-UHFFFAOYSA-N Butyric acid Chemical compound CCCC(O)=O FERIUCNNQQJTOY-UHFFFAOYSA-N 0.000 description 11
- 230000001276 controlling effect Effects 0.000 description 11
- 101000611183 Homo sapiens Tumor necrosis factor Proteins 0.000 description 10
- 235000001014 amino acid Nutrition 0.000 description 10
- 229940024606 amino acid Drugs 0.000 description 10
- 150000001413 amino acids Chemical class 0.000 description 10
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 10
- 230000010261 cell growth Effects 0.000 description 10
- 229920001184 polypeptide Polymers 0.000 description 10
- 125000005629 sialic acid group Chemical group 0.000 description 10
- OVRNDRQMDRJTHS-RTRLPJTCSA-N N-acetyl-D-glucosamine Chemical compound CC(=O)N[C@H]1C(O)O[C@H](CO)[C@@H](O)[C@@H]1O OVRNDRQMDRJTHS-RTRLPJTCSA-N 0.000 description 9
- 239000001888 Peptone Substances 0.000 description 9
- 108010080698 Peptones Proteins 0.000 description 9
- 102100040247 Tumor necrosis factor Human genes 0.000 description 9
- 230000000694 effects Effects 0.000 description 9
- 239000008103 glucose Substances 0.000 description 9
- 239000003102 growth factor Substances 0.000 description 9
- 235000019319 peptone Nutrition 0.000 description 9
- 230000007704 transition Effects 0.000 description 9
- 239000000872 buffer Substances 0.000 description 8
- FDGQSTZJBFJUBT-UHFFFAOYSA-N hypoxanthine Chemical compound O=C1NC=NC2=C1NC=N2 FDGQSTZJBFJUBT-UHFFFAOYSA-N 0.000 description 8
- 239000000243 solution Substances 0.000 description 8
- FERIUCNNQQJTOY-UHFFFAOYSA-M Butyrate Chemical compound CCCC([O-])=O FERIUCNNQQJTOY-UHFFFAOYSA-M 0.000 description 7
- WQZGKKKJIJFFOK-QTVWNMPRSA-N D-mannopyranose Chemical compound OC[C@H]1OC(O)[C@@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-QTVWNMPRSA-N 0.000 description 7
- 239000000306 component Substances 0.000 description 7
- 230000014509 gene expression Effects 0.000 description 7
- 235000000346 sugar Nutrition 0.000 description 7
- 230000014616 translation Effects 0.000 description 7
- DWRXFEITVBNRMK-UHFFFAOYSA-N Beta-D-1-Arabinofuranosylthymine Natural products O=C1NC(=O)C(C)=CN1C1C(O)C(O)C(CO)O1 DWRXFEITVBNRMK-UHFFFAOYSA-N 0.000 description 6
- 108020004414 DNA Proteins 0.000 description 6
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 6
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 6
- 238000004458 analytical method Methods 0.000 description 6
- IQFYYKKMVGJFEH-UHFFFAOYSA-N beta-L-thymidine Natural products O=C1NC(=O)C(C)=CN1C1OC(CO)C(O)C1 IQFYYKKMVGJFEH-UHFFFAOYSA-N 0.000 description 6
- 230000007423 decrease Effects 0.000 description 6
- 238000009472 formulation Methods 0.000 description 6
- 150000008163 sugars Chemical class 0.000 description 6
- 229940104230 thymidine Drugs 0.000 description 6
- 102000004190 Enzymes Human genes 0.000 description 5
- 108090000790 Enzymes Proteins 0.000 description 5
- 229910019142 PO4 Inorganic materials 0.000 description 5
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 5
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 5
- 102000003838 Sialyltransferases Human genes 0.000 description 5
- 108090000141 Sialyltransferases Proteins 0.000 description 5
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 5
- 150000007513 acids Chemical class 0.000 description 5
- 238000003556 assay Methods 0.000 description 5
- 229940088598 enzyme Drugs 0.000 description 5
- 108020001507 fusion proteins Proteins 0.000 description 5
- 102000037865 fusion proteins Human genes 0.000 description 5
- 230000013595 glycosylation Effects 0.000 description 5
- 239000000463 material Substances 0.000 description 5
- 235000015097 nutrients Nutrition 0.000 description 5
- 239000010452 phosphate Substances 0.000 description 5
- 238000000746 purification Methods 0.000 description 5
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 4
- OAKJQQAXSVQMHS-UHFFFAOYSA-N Hydrazine Chemical compound NN OAKJQQAXSVQMHS-UHFFFAOYSA-N 0.000 description 4
- UGQMRVRMYYASKQ-UHFFFAOYSA-N Hypoxanthine nucleoside Natural products OC1C(O)C(CO)OC1N1C(NC=NC2=O)=C2N=C1 UGQMRVRMYYASKQ-UHFFFAOYSA-N 0.000 description 4
- 102100029268 Neurotrophin-3 Human genes 0.000 description 4
- DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 4
- OIRDTQYFTABQOQ-KQYNXXCUSA-N adenosine Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@@H]1O[C@H](CO)[C@@H](O)[C@H]1O OIRDTQYFTABQOQ-KQYNXXCUSA-N 0.000 description 4
- 210000004369 blood Anatomy 0.000 description 4
- 239000008280 blood Substances 0.000 description 4
- 238000012511 carbohydrate analysis Methods 0.000 description 4
- 239000003814 drug Substances 0.000 description 4
- 238000006206 glycosylation reaction Methods 0.000 description 4
- 229940088597 hormone Drugs 0.000 description 4
- 239000005556 hormone Substances 0.000 description 4
- 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 4
- 210000003292 kidney cell Anatomy 0.000 description 4
- JVTAAEKCZFNVCJ-UHFFFAOYSA-N lactic acid Chemical compound CC(O)C(O)=O JVTAAEKCZFNVCJ-UHFFFAOYSA-N 0.000 description 4
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 4
- 150000003839 salts Chemical class 0.000 description 4
- 239000000523 sample Substances 0.000 description 4
- 239000000126 substance Substances 0.000 description 4
- 238000012360 testing method Methods 0.000 description 4
- 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 3
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 3
- HNSDLXPSAYFUHK-UHFFFAOYSA-N 1,4-bis(2-ethylhexyl) sulfosuccinate Chemical compound CCCCC(CC)COC(=O)CC(S(O)(=O)=O)C(=O)OCC(CC)CCCC HNSDLXPSAYFUHK-UHFFFAOYSA-N 0.000 description 3
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 3
- 102000004127 Cytokines Human genes 0.000 description 3
- 108090000695 Cytokines Proteins 0.000 description 3
- 102100024746 Dihydrofolate reductase Human genes 0.000 description 3
- 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 3
- 239000004471 Glycine Substances 0.000 description 3
- 101000976075 Homo sapiens Insulin Proteins 0.000 description 3
- 102000004877 Insulin Human genes 0.000 description 3
- 108090001061 Insulin Proteins 0.000 description 3
- FYYHWMGAXLPEAU-UHFFFAOYSA-N Magnesium Chemical compound [Mg] FYYHWMGAXLPEAU-UHFFFAOYSA-N 0.000 description 3
- 108010025020 Nerve Growth Factor Proteins 0.000 description 3
- 206010040070 Septic Shock Diseases 0.000 description 3
- 102000004887 Transforming Growth Factor beta Human genes 0.000 description 3
- 108090001012 Transforming Growth Factor beta Proteins 0.000 description 3
- 239000006143 cell culture medium Substances 0.000 description 3
- 238000011098 chromatofocusing Methods 0.000 description 3
- 238000004587 chromatography analysis Methods 0.000 description 3
- 108020001096 dihydrofolate reductase Proteins 0.000 description 3
- 230000004927 fusion Effects 0.000 description 3
- 229930182830 galactose Natural products 0.000 description 3
- 238000001030 gas--liquid chromatography Methods 0.000 description 3
- 230000001900 immune effect Effects 0.000 description 3
- 238000000338 in vitro Methods 0.000 description 3
- 238000001727 in vivo Methods 0.000 description 3
- 239000002054 inoculum Substances 0.000 description 3
- 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 3
- 150000002632 lipids Chemical class 0.000 description 3
- 230000001404 mediated effect Effects 0.000 description 3
- 230000004048 modification Effects 0.000 description 3
- 238000012986 modification Methods 0.000 description 3
- 238000010369 molecular cloning Methods 0.000 description 3
- 150000002772 monosaccharides Chemical class 0.000 description 3
- 230000002035 prolonged effect Effects 0.000 description 3
- 239000011780 sodium chloride Substances 0.000 description 3
- ZRKFYGHZFMAOKI-QMGMOQQFSA-N tgfbeta Chemical compound C([C@H](NC(=O)[C@H](C(C)C)NC(=O)CNC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CC(C)C)NC(=O)CNC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)CCSC)C(C)C)[C@@H](C)CC)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](C)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N1[C@@H](CCC1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(O)=O)C1=CC=C(O)C=C1 ZRKFYGHZFMAOKI-QMGMOQQFSA-N 0.000 description 3
- VBEQCZHXXJYVRD-GACYYNSASA-N uroanthelone Chemical compound C([C@@H](C(=O)N[C@H](C(=O)N[C@@H](CS)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CS)C(=O)N[C@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)NCC(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O)C(C)C)[C@@H](C)O)NC(=O)[C@H](CO)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@H](CCSC)NC(=O)[C@H](CS)NC(=O)[C@@H](NC(=O)CNC(=O)CNC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CS)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CS)NC(=O)CNC(=O)[C@H]1N(CCC1)C(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC(N)=O)C(C)C)[C@@H](C)CC)C1=CC=C(O)C=C1 VBEQCZHXXJYVRD-GACYYNSASA-N 0.000 description 3
- 239000011782 vitamin Substances 0.000 description 3
- 235000013343 vitamin Nutrition 0.000 description 3
- 229940088594 vitamin Drugs 0.000 description 3
- 229930003231 vitamin Natural products 0.000 description 3
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 3
- 108010088751 Albumins Proteins 0.000 description 2
- 102000009027 Albumins Human genes 0.000 description 2
- QGZKDVFQNNGYKY-UHFFFAOYSA-N Ammonia Chemical compound N QGZKDVFQNNGYKY-UHFFFAOYSA-N 0.000 description 2
- 241000283690 Bos taurus Species 0.000 description 2
- 239000002126 C01EB10 - Adenosine Substances 0.000 description 2
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 2
- 241000282693 Cercopithecidae Species 0.000 description 2
- 241000699802 Cricetulus griseus Species 0.000 description 2
- SHZGCJCMOBCMKK-UHFFFAOYSA-N D-mannomethylose Natural products CC1OC(O)C(O)C(O)C1O SHZGCJCMOBCMKK-UHFFFAOYSA-N 0.000 description 2
- 102400001368 Epidermal growth factor Human genes 0.000 description 2
- 101800003838 Epidermal growth factor Proteins 0.000 description 2
- PNNNRSAQSRJVSB-SLPGGIOYSA-N Fucose Natural products C[C@H](O)[C@@H](O)[C@H](O)[C@H](O)C=O PNNNRSAQSRJVSB-SLPGGIOYSA-N 0.000 description 2
- CEAZRRDELHUEMR-URQXQFDESA-N Gentamicin Chemical compound O1[C@H](C(C)NC)CC[C@@H](N)[C@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](NC)[C@@](C)(O)CO2)O)[C@H](N)C[C@@H]1N CEAZRRDELHUEMR-URQXQFDESA-N 0.000 description 2
- 229930182566 Gentamicin Natural products 0.000 description 2
- 108090000723 Insulin-Like Growth Factor I Proteins 0.000 description 2
- 102000004218 Insulin-Like Growth Factor I Human genes 0.000 description 2
- SHZGCJCMOBCMKK-DHVFOXMCSA-N L-fucopyranose Chemical compound C[C@@H]1OC(O)[C@@H](O)[C@H](O)[C@@H]1O SHZGCJCMOBCMKK-DHVFOXMCSA-N 0.000 description 2
- FBOZXECLQNJBKD-ZDUSSCGKSA-N L-methotrexate Chemical compound C=1N=C2N=C(N)N=C(N)C2=NC=1CN(C)C1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 FBOZXECLQNJBKD-ZDUSSCGKSA-N 0.000 description 2
- 108010090665 Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase Proteins 0.000 description 2
- 241001465754 Metazoa Species 0.000 description 2
- SQVRNKJHWKZAKO-PFQGKNLYSA-N N-acetyl-beta-neuraminic acid Chemical compound CC(=O)N[C@@H]1[C@@H](O)C[C@@](O)(C(O)=O)O[C@H]1[C@H](O)[C@H](O)CO SQVRNKJHWKZAKO-PFQGKNLYSA-N 0.000 description 2
- 206010028851 Necrosis Diseases 0.000 description 2
- 102000005348 Neuraminidase Human genes 0.000 description 2
- 108010006232 Neuraminidase Proteins 0.000 description 2
- 108090000742 Neurotrophin 3 Proteins 0.000 description 2
- 241000700159 Rattus Species 0.000 description 2
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 2
- 239000004473 Threonine Substances 0.000 description 2
- 102100033571 Tissue-type plasminogen activator Human genes 0.000 description 2
- 101150009046 Tnfrsf1a gene Proteins 0.000 description 2
- 244000000188 Vaccinium ovalifolium Species 0.000 description 2
- 230000002378 acidificating effect Effects 0.000 description 2
- 239000000654 additive Substances 0.000 description 2
- 229960005305 adenosine Drugs 0.000 description 2
- 235000021120 animal protein Nutrition 0.000 description 2
- 238000013459 approach Methods 0.000 description 2
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 2
- 239000007640 basal medium Substances 0.000 description 2
- 210000000988 bone and bone Anatomy 0.000 description 2
- 239000011575 calcium Substances 0.000 description 2
- 229910052791 calcium Inorganic materials 0.000 description 2
- 125000004432 carbon atom Chemical group C* 0.000 description 2
- 239000000470 constituent Substances 0.000 description 2
- 239000000356 contaminant Substances 0.000 description 2
- 201000010099 disease Diseases 0.000 description 2
- 229940079593 drug Drugs 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 229940116977 epidermal growth factor Drugs 0.000 description 2
- HQPMKSGTIOYHJT-UHFFFAOYSA-N ethane-1,2-diol;propane-1,2-diol Chemical compound OCCO.CC(O)CO HQPMKSGTIOYHJT-UHFFFAOYSA-N 0.000 description 2
- 239000012634 fragment Substances 0.000 description 2
- 239000012737 fresh medium Substances 0.000 description 2
- 238000005227 gel permeation chromatography Methods 0.000 description 2
- 229930182470 glycoside Natural products 0.000 description 2
- 238000003119 immunoblot Methods 0.000 description 2
- 230000002401 inhibitory effect Effects 0.000 description 2
- 229940125396 insulin Drugs 0.000 description 2
- 238000005342 ion exchange Methods 0.000 description 2
- 150000002500 ions Chemical class 0.000 description 2
- 210000003734 kidney Anatomy 0.000 description 2
- 239000004310 lactic acid Substances 0.000 description 2
- 235000014655 lactic acid Nutrition 0.000 description 2
- 210000005229 liver cell Anatomy 0.000 description 2
- 239000012092 media component Substances 0.000 description 2
- 239000012528 membrane Substances 0.000 description 2
- 108020004999 messenger RNA Proteins 0.000 description 2
- 229960000485 methotrexate Drugs 0.000 description 2
- 230000017074 necrotic cell death Effects 0.000 description 2
- 239000003900 neurotrophic factor Substances 0.000 description 2
- 230000007935 neutral effect Effects 0.000 description 2
- 239000002777 nucleoside Substances 0.000 description 2
- 125000003835 nucleoside group Chemical group 0.000 description 2
- 210000001672 ovary Anatomy 0.000 description 2
- 229910052760 oxygen Inorganic materials 0.000 description 2
- 239000001301 oxygen Substances 0.000 description 2
- 230000010412 perfusion Effects 0.000 description 2
- 239000013612 plasmid Substances 0.000 description 2
- 229920001993 poloxamer 188 Polymers 0.000 description 2
- 239000003223 protective agent Substances 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 206010039073 rheumatoid arthritis Diseases 0.000 description 2
- 230000036303 septic shock Effects 0.000 description 2
- 238000003860 storage Methods 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- 238000004114 suspension culture Methods 0.000 description 2
- 230000003612 virological effect Effects 0.000 description 2
- LHZGINQTXBBMKG-PYHIIVFHSA-N (4S,5R,6R)-5-amino-2,4-dihydroxy-5-(2-hydroxyacetyl)-6-[(1R,2R)-1,2,3-trihydroxypropyl]oxane-2-carboxylic acid Chemical compound OCC(=O)[C@@]1(N)[C@@H](O)CC(O)(C(O)=O)O[C@H]1[C@H](O)[C@H](O)CO LHZGINQTXBBMKG-PYHIIVFHSA-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
- 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
- 208000030507 AIDS Diseases 0.000 description 1
- 102000005606 Activins Human genes 0.000 description 1
- 108010059616 Activins Proteins 0.000 description 1
- 244000105975 Antidesma platyphyllum Species 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
- 101800001288 Atrial natriuretic factor Proteins 0.000 description 1
- 102400001282 Atrial natriuretic peptide Human genes 0.000 description 1
- 101800001890 Atrial natriuretic peptide Proteins 0.000 description 1
- 208000023275 Autoimmune disease Diseases 0.000 description 1
- 101000959414 Bacillus thermoamyloliquefaciens Alpha-glucosidase 2 Proteins 0.000 description 1
- 208000031729 Bacteremia Diseases 0.000 description 1
- 102100026189 Beta-galactosidase Human genes 0.000 description 1
- 239000002028 Biomass Substances 0.000 description 1
- 108010039209 Blood Coagulation Factors Proteins 0.000 description 1
- 102000015081 Blood Coagulation Factors Human genes 0.000 description 1
- 102000013585 Bombesin Human genes 0.000 description 1
- 108010051479 Bombesin Proteins 0.000 description 1
- 206010006187 Breast cancer Diseases 0.000 description 1
- 108010041884 CD4 Immunoadhesins Proteins 0.000 description 1
- 102000055006 Calcitonin Human genes 0.000 description 1
- 108060001064 Calcitonin Proteins 0.000 description 1
- 241000282465 Canis Species 0.000 description 1
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 1
- CURLTUGMZLYLDI-UHFFFAOYSA-N Carbon dioxide Chemical compound O=C=O CURLTUGMZLYLDI-UHFFFAOYSA-N 0.000 description 1
- 102000014914 Carrier Proteins Human genes 0.000 description 1
- 108010078791 Carrier Proteins Proteins 0.000 description 1
- 241000282552 Chlorocebus aethiops Species 0.000 description 1
- 235000008733 Citrus aurantifolia Nutrition 0.000 description 1
- 102100022641 Coagulation factor IX Human genes 0.000 description 1
- 108091026890 Coding region Proteins 0.000 description 1
- 241000699800 Cricetinae Species 0.000 description 1
- 208000011231 Crohn disease Diseases 0.000 description 1
- 101710088194 Dehydrogenase Proteins 0.000 description 1
- 102000016911 Deoxyribonucleases Human genes 0.000 description 1
- 108010053770 Deoxyribonucleases Proteins 0.000 description 1
- MYMOFIZGZYHOMD-UHFFFAOYSA-N Dioxygen Chemical compound O=O MYMOFIZGZYHOMD-UHFFFAOYSA-N 0.000 description 1
- 108090000204 Dipeptidase 1 Proteins 0.000 description 1
- 108010089072 Dolichyl-diphosphooligosaccharide-protein glycotransferase Proteins 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 206010014824 Endotoxic shock Diseases 0.000 description 1
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 1
- 241001421147 Evenus Species 0.000 description 1
- 108010076282 Factor IX Proteins 0.000 description 1
- 108050007372 Fibroblast Growth Factor Proteins 0.000 description 1
- 102000018233 Fibroblast Growth Factor Human genes 0.000 description 1
- 108090000386 Fibroblast Growth Factor 1 Proteins 0.000 description 1
- 102100031706 Fibroblast growth factor 1 Human genes 0.000 description 1
- 102100024785 Fibroblast growth factor 2 Human genes 0.000 description 1
- 108090000379 Fibroblast growth factor 2 Proteins 0.000 description 1
- 102000012673 Follicle Stimulating Hormone Human genes 0.000 description 1
- 108010079345 Follicle Stimulating Hormone Proteins 0.000 description 1
- 108010019236 Fucosyltransferases Proteins 0.000 description 1
- 102000006471 Fucosyltransferases Human genes 0.000 description 1
- 108010010803 Gelatin Proteins 0.000 description 1
- 102400000321 Glucagon Human genes 0.000 description 1
- 108060003199 Glucagon Proteins 0.000 description 1
- 101710127404 Glycoprotein 3 Proteins 0.000 description 1
- 108010051696 Growth Hormone Proteins 0.000 description 1
- 102000018997 Growth Hormone Human genes 0.000 description 1
- 239000000095 Growth Hormone-Releasing Hormone Substances 0.000 description 1
- 239000007995 HEPES buffer Substances 0.000 description 1
- 101100005713 Homo sapiens CD4 gene Proteins 0.000 description 1
- 101000599951 Homo sapiens Insulin-like growth factor I Proteins 0.000 description 1
- 101000904196 Homo sapiens Pancreatic secretory granule membrane major glycoprotein GP2 Proteins 0.000 description 1
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 1
- 108010000521 Human Growth Hormone Proteins 0.000 description 1
- 102000002265 Human Growth Hormone Human genes 0.000 description 1
- 239000000854 Human Growth Hormone Substances 0.000 description 1
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 1
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 1
- 108090001117 Insulin-Like Growth Factor II Proteins 0.000 description 1
- 102000048143 Insulin-Like Growth Factor II Human genes 0.000 description 1
- 102100037852 Insulin-like growth factor I Human genes 0.000 description 1
- 102000006992 Interferon-alpha Human genes 0.000 description 1
- 108010047761 Interferon-alpha Proteins 0.000 description 1
- 102000014150 Interferons Human genes 0.000 description 1
- 108010050904 Interferons Proteins 0.000 description 1
- 108050006617 Interleukin-1 receptor Proteins 0.000 description 1
- 102000019223 Interleukin-1 receptor Human genes 0.000 description 1
- 102000010789 Interleukin-2 Receptors Human genes 0.000 description 1
- 108010038453 Interleukin-2 Receptors Proteins 0.000 description 1
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 1
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 1
- 108010059881 Lactase Proteins 0.000 description 1
- 108090001090 Lectins Proteins 0.000 description 1
- 102000004856 Lectins Human genes 0.000 description 1
- DUKURNFHYQXCJG-UHFFFAOYSA-N Lewis A pentasaccharide Natural products OC1C(O)C(O)C(C)OC1OC1C(OC2C(C(O)C(O)C(CO)O2)O)C(NC(C)=O)C(OC2C(C(OC3C(OC(O)C(O)C3O)CO)OC(CO)C2O)O)OC1CO DUKURNFHYQXCJG-UHFFFAOYSA-N 0.000 description 1
- 108090001030 Lipoproteins Proteins 0.000 description 1
- 102000004895 Lipoproteins Human genes 0.000 description 1
- 102000009151 Luteinizing Hormone Human genes 0.000 description 1
- 108010073521 Luteinizing Hormone Proteins 0.000 description 1
- 102000004083 Lymphotoxin-alpha Human genes 0.000 description 1
- 108090000542 Lymphotoxin-alpha Proteins 0.000 description 1
- 108010046938 Macrophage Colony-Stimulating Factor Proteins 0.000 description 1
- 102000009571 Macrophage Inflammatory Proteins Human genes 0.000 description 1
- 108010009474 Macrophage Inflammatory Proteins Proteins 0.000 description 1
- 102100028123 Macrophage colony-stimulating factor 1 Human genes 0.000 description 1
- 241000124008 Mammalia Species 0.000 description 1
- 108010031099 Mannose Receptor Proteins 0.000 description 1
- 108010052285 Membrane Proteins Proteins 0.000 description 1
- 206010027476 Metastases Diseases 0.000 description 1
- 101710151805 Mitochondrial intermediate peptidase 1 Proteins 0.000 description 1
- 241001529936 Murinae Species 0.000 description 1
- 101100341510 Mus musculus Itgal gene Proteins 0.000 description 1
- 101100425758 Mus musculus Tnfrsf1b gene Proteins 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
- FDJKUWYYUZCUJX-PGIATKPXSA-M N-glycoloylneuraminate Chemical compound OC[C@@H](O)[C@@H](O)[C@@H]1OC(O)(C([O-])=O)C[C@H](O)[C@H]1NC(=O)CO FDJKUWYYUZCUJX-PGIATKPXSA-M 0.000 description 1
- 230000004988 N-glycosylation Effects 0.000 description 1
- 102000003729 Neprilysin Human genes 0.000 description 1
- 108090000028 Neprilysin Proteins 0.000 description 1
- 102000015336 Nerve Growth Factor Human genes 0.000 description 1
- 239000000020 Nitrocellulose Substances 0.000 description 1
- 108091028043 Nucleic acid sequence Proteins 0.000 description 1
- 102100024019 Pancreatic secretory granule membrane major glycoprotein GP2 Human genes 0.000 description 1
- 102000003982 Parathyroid hormone Human genes 0.000 description 1
- 108090000445 Parathyroid hormone Proteins 0.000 description 1
- 102000003992 Peroxidases Human genes 0.000 description 1
- 102000004160 Phosphoric Monoester Hydrolases Human genes 0.000 description 1
- 108090000608 Phosphoric Monoester Hydrolases Proteins 0.000 description 1
- 108010004434 Primatone RL Proteins 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 229940124158 Protease/peptidase inhibitor Drugs 0.000 description 1
- 101800004937 Protein C Proteins 0.000 description 1
- 239000012980 RPMI-1640 medium Substances 0.000 description 1
- 241000700157 Rattus norvegicus Species 0.000 description 1
- 108090000103 Relaxin Proteins 0.000 description 1
- 102000003743 Relaxin Human genes 0.000 description 1
- 102400000610 Relaxin B chain Human genes 0.000 description 1
- 101710109558 Relaxin B chain Proteins 0.000 description 1
- 102100028255 Renin Human genes 0.000 description 1
- 108090000783 Renin Proteins 0.000 description 1
- 102400000827 Saposin-D Human genes 0.000 description 1
- 101800001700 Saposin-D Proteins 0.000 description 1
- 229920005654 Sephadex Polymers 0.000 description 1
- 239000012507 Sephadex™ Substances 0.000 description 1
- 229920002684 Sepharose Polymers 0.000 description 1
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 1
- 102100022831 Somatoliberin Human genes 0.000 description 1
- 101710142969 Somatoliberin Proteins 0.000 description 1
- 241000583281 Sugiura Species 0.000 description 1
- 102000019197 Superoxide Dismutase Human genes 0.000 description 1
- 108010012715 Superoxide dismutase Proteins 0.000 description 1
- 108091008874 T cell receptors Proteins 0.000 description 1
- 102000016266 T-Cell Antigen Receptors Human genes 0.000 description 1
- 210000001744 T-lymphocyte Anatomy 0.000 description 1
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 1
- 108010022394 Threonine synthase Proteins 0.000 description 1
- 108090000190 Thrombin Proteins 0.000 description 1
- 108010000499 Thromboplastin Proteins 0.000 description 1
- 102000002262 Thromboplastin Human genes 0.000 description 1
- 235000011941 Tilia x europaea Nutrition 0.000 description 1
- 108090000373 Tissue Plasminogen Activator Proteins 0.000 description 1
- 108050006955 Tissue-type plasminogen activator Proteins 0.000 description 1
- 102000004338 Transferrin Human genes 0.000 description 1
- 108090000901 Transferrin Proteins 0.000 description 1
- 102400001320 Transforming growth factor alpha Human genes 0.000 description 1
- 101800004564 Transforming growth factor alpha Proteins 0.000 description 1
- 206010052779 Transplant rejections Diseases 0.000 description 1
- 239000007983 Tris buffer Substances 0.000 description 1
- 102000003990 Urokinase-type plasminogen activator Human genes 0.000 description 1
- 108090000435 Urokinase-type plasminogen activator Proteins 0.000 description 1
- ZYPGADGCNXOUJP-CXVPHVKISA-N Variotin Chemical compound CCCC[C@@H](O)\C=C(/C)\C=C\C=C\C(=O)N1CCCC1=O ZYPGADGCNXOUJP-CXVPHVKISA-N 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- 238000006640 acetylation reaction Methods 0.000 description 1
- 238000005903 acid hydrolysis reaction Methods 0.000 description 1
- 239000012190 activator Substances 0.000 description 1
- 239000000488 activin Substances 0.000 description 1
- 230000006978 adaptation Effects 0.000 description 1
- 230000000996 additive effect Effects 0.000 description 1
- 229910021529 ammonia Inorganic materials 0.000 description 1
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 1
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 1
- 235000011130 ammonium sulphate Nutrition 0.000 description 1
- 238000004873 anchoring Methods 0.000 description 1
- 210000004102 animal cell Anatomy 0.000 description 1
- 238000010171 animal model Methods 0.000 description 1
- 238000005349 anion exchange Methods 0.000 description 1
- 238000005571 anion exchange chromatography Methods 0.000 description 1
- 150000001450 anions Chemical class 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 229940088710 antibiotic agent Drugs 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- 235000009582 asparagine Nutrition 0.000 description 1
- 229960001230 asparagine Drugs 0.000 description 1
- 125000000613 asparagine group Chemical group N[C@@H](CC(N)=O)C(=O)* 0.000 description 1
- 235000003704 aspartic acid Nutrition 0.000 description 1
- 230000001363 autoimmune Effects 0.000 description 1
- 108010005774 beta-Galactosidase Proteins 0.000 description 1
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 1
- 102000006635 beta-lactamase Human genes 0.000 description 1
- 238000010364 biochemical engineering Methods 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 239000003114 blood coagulation factor Substances 0.000 description 1
- DNDCVAGJPBKION-DOPDSADYSA-N bombesin Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCSC)C(N)=O)NC(=O)CNC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H](CC=1NC2=CC=CC=C2C=1)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)CNC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H]1NC(=O)CC1)C(C)C)C1=CN=CN1 DNDCVAGJPBKION-DOPDSADYSA-N 0.000 description 1
- 108010006025 bovine growth hormone Proteins 0.000 description 1
- 210000004556 brain Anatomy 0.000 description 1
- 239000007975 buffered saline Substances 0.000 description 1
- 239000006227 byproduct Substances 0.000 description 1
- BBBFJLBPOGFECG-VJVYQDLKSA-N calcitonin Chemical compound N([C@H](C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H]([C@@H](C)O)C(=O)N1[C@@H](CCC1)C(N)=O)C(C)C)C(=O)[C@@H]1CSSC[C@H](N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1 BBBFJLBPOGFECG-VJVYQDLKSA-N 0.000 description 1
- 229960004015 calcitonin Drugs 0.000 description 1
- 239000001506 calcium phosphate Substances 0.000 description 1
- 229910000389 calcium phosphate Inorganic materials 0.000 description 1
- 235000011010 calcium phosphates Nutrition 0.000 description 1
- 229910052799 carbon Inorganic materials 0.000 description 1
- 235000011089 carbon dioxide Nutrition 0.000 description 1
- NSQLIUXCMFBZME-MPVJKSABSA-N carperitide Chemical compound C([C@H]1C(=O)NCC(=O)NCC(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C(NCC(=O)N[C@@H](C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CSSC[C@@H](C(=O)N1)NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(O)=O)=O)[C@@H](C)CC)C1=CC=CC=C1 NSQLIUXCMFBZME-MPVJKSABSA-N 0.000 description 1
- 238000005341 cation exchange Methods 0.000 description 1
- 238000012832 cell culture technique Methods 0.000 description 1
- 230000032823 cell division Effects 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 238000002648 combination therapy Methods 0.000 description 1
- 238000004891 communication Methods 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 238000001816 cooling Methods 0.000 description 1
- 239000012531 culture fluid Substances 0.000 description 1
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 1
- 238000001212 derivatisation Methods 0.000 description 1
- 239000003599 detergent Substances 0.000 description 1
- 239000008121 dextrose Substances 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- 238000000502 dialysis Methods 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 102000004419 dihydrofolate reductase Human genes 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- AIUDWMLXCFRVDR-UHFFFAOYSA-N dimethyl 2-(3-ethyl-3-methylpentyl)propanedioate Chemical class CCC(C)(CC)CCC(C(=O)OC)C(=O)OC AIUDWMLXCFRVDR-UHFFFAOYSA-N 0.000 description 1
- 229910001882 dioxygen Inorganic materials 0.000 description 1
- IZEKFCXSFNUWAM-UHFFFAOYSA-N dipyridamole Chemical compound C=12N=C(N(CCO)CCO)N=C(N3CCCCC3)C2=NC(N(CCO)CCO)=NC=1N1CCCCC1 IZEKFCXSFNUWAM-UHFFFAOYSA-N 0.000 description 1
- 208000037765 diseases and disorders Diseases 0.000 description 1
- 238000005538 encapsulation Methods 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- 230000006353 environmental stress Effects 0.000 description 1
- 230000006862 enzymatic digestion Effects 0.000 description 1
- 239000013613 expression plasmid Substances 0.000 description 1
- 239000013604 expression vector Substances 0.000 description 1
- 229960004222 factor ix Drugs 0.000 description 1
- 230000002349 favourable effect Effects 0.000 description 1
- 239000012527 feed solution Substances 0.000 description 1
- 229940126864 fibroblast growth factor Drugs 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 229940028334 follicle stimulating hormone Drugs 0.000 description 1
- 238000004108 freeze drying Methods 0.000 description 1
- 230000005714 functional activity Effects 0.000 description 1
- 108010042430 galactose receptor Proteins 0.000 description 1
- 239000007789 gas Substances 0.000 description 1
- 239000000499 gel Substances 0.000 description 1
- 239000008273 gelatin Substances 0.000 description 1
- 229920000159 gelatin Polymers 0.000 description 1
- 235000019322 gelatine Nutrition 0.000 description 1
- 235000011852 gelatine desserts Nutrition 0.000 description 1
- 238000002523 gelfiltration Methods 0.000 description 1
- MASNOZXLGMXCHN-ZLPAWPGGSA-N glucagon Chemical compound C([C@@H](C(=O)N[C@H](C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(O)=O)C(C)C)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CO)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CO)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)[C@@H](NC(=O)CNC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC=1NC=NC=1)[C@@H](C)O)[C@@H](C)O)C1=CC=CC=C1 MASNOZXLGMXCHN-ZLPAWPGGSA-N 0.000 description 1
- 229960004666 glucagon Drugs 0.000 description 1
- 108010050669 glucosidase I Proteins 0.000 description 1
- 150000004676 glycans Chemical class 0.000 description 1
- 150000002337 glycosamines Chemical class 0.000 description 1
- 150000002338 glycosides Chemical class 0.000 description 1
- 239000000122 growth hormone Substances 0.000 description 1
- 235000009424 haa Nutrition 0.000 description 1
- 238000003306 harvesting Methods 0.000 description 1
- 230000002607 hemopoietic effect Effects 0.000 description 1
- 206010073071 hepatocellular carcinoma Diseases 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- 239000012510 hollow fiber Substances 0.000 description 1
- 102000057041 human TNF Human genes 0.000 description 1
- 238000009396 hybridization Methods 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 208000026278 immune system disease Diseases 0.000 description 1
- 230000002163 immunogen Effects 0.000 description 1
- 230000002637 immunotoxin Effects 0.000 description 1
- 229940051026 immunotoxin Drugs 0.000 description 1
- 239000002596 immunotoxin Substances 0.000 description 1
- 231100000608 immunotoxin Toxicity 0.000 description 1
- 208000027866 inflammatory disease Diseases 0.000 description 1
- 238000001802 infusion Methods 0.000 description 1
- 239000000893 inhibin Substances 0.000 description 1
- ZPNFWUPYTFPOJU-LPYSRVMUSA-N iniprol Chemical compound C([C@H]1C(=O)NCC(=O)NCC(=O)N[C@H]2CSSC[C@H]3C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C(N[C@H](C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC=4C=CC=CC=4)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC=4C=CC=CC=4)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC2=O)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC=2C=CC=CC=2)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H]2N(CCC2)C(=O)[C@@H](N)CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N2[C@@H](CCC2)C(=O)N2[C@@H](CCC2)C(=O)N[C@@H](CC=2C=CC(O)=CC=2)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N2[C@@H](CCC2)C(=O)N3)C(=O)NCC(=O)NCC(=O)N[C@@H](C)C(O)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@H](C(=O)N1)C(C)C)[C@@H](C)O)[C@@H](C)CC)=O)[C@@H](C)CC)C1=CC=C(O)C=C1 ZPNFWUPYTFPOJU-LPYSRVMUSA-N 0.000 description 1
- 230000000977 initiatory effect Effects 0.000 description 1
- 239000007972 injectable composition Substances 0.000 description 1
- 238000002347 injection Methods 0.000 description 1
- 239000007924 injection Substances 0.000 description 1
- 238000011081 inoculation Methods 0.000 description 1
- 150000002484 inorganic compounds Chemical class 0.000 description 1
- 229910010272 inorganic material Inorganic materials 0.000 description 1
- 229940079322 interferon Drugs 0.000 description 1
- 238000001990 intravenous administration Methods 0.000 description 1
- 230000009545 invasion Effects 0.000 description 1
- 238000001155 isoelectric focusing Methods 0.000 description 1
- 229940116108 lactase Drugs 0.000 description 1
- 239000002523 lectin Substances 0.000 description 1
- 239000004571 lime Substances 0.000 description 1
- 239000003589 local anesthetic agent Substances 0.000 description 1
- 229960005015 local anesthetics Drugs 0.000 description 1
- 210000005265 lung cell Anatomy 0.000 description 1
- 229940066294 lung surfactant Drugs 0.000 description 1
- 239000003580 lung surfactant Substances 0.000 description 1
- 206010025135 lupus erythematosus Diseases 0.000 description 1
- 229940040129 luteinizing hormone Drugs 0.000 description 1
- 210000002751 lymph Anatomy 0.000 description 1
- 239000006166 lysate Substances 0.000 description 1
- 238000004949 mass spectrometry Methods 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 239000013028 medium composition Substances 0.000 description 1
- 230000009401 metastasis Effects 0.000 description 1
- MYWUZJCMWCOHBA-VIFPVBQESA-N methamphetamine Chemical compound CN[C@@H](C)CC1=CC=CC=C1 MYWUZJCMWCOHBA-VIFPVBQESA-N 0.000 description 1
- 125000002496 methyl group Chemical group [H]C([H])([H])* 0.000 description 1
- 125000004170 methylsulfonyl group Chemical group [H]C([H])([H])S(*)(=O)=O 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 238000004264 monolayer culture Methods 0.000 description 1
- 238000002703 mutagenesis Methods 0.000 description 1
- 231100000350 mutagenesis Toxicity 0.000 description 1
- 229940053128 nerve growth factor Drugs 0.000 description 1
- 229940032018 neurotrophin 3 Drugs 0.000 description 1
- 229920001220 nitrocellulos Polymers 0.000 description 1
- -1 oligosaccharide carbohydrate Chemical class 0.000 description 1
- 150000007524 organic acids Chemical class 0.000 description 1
- 235000005985 organic acids Nutrition 0.000 description 1
- 150000002894 organic compounds Chemical class 0.000 description 1
- 230000003204 osmotic effect Effects 0.000 description 1
- 230000002138 osteoinductive effect Effects 0.000 description 1
- 230000001590 oxidative effect Effects 0.000 description 1
- 239000000199 parathyroid hormone Substances 0.000 description 1
- 229960001319 parathyroid hormone Drugs 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 239000000137 peptide hydrolase inhibitor Substances 0.000 description 1
- 229940066779 peptones Drugs 0.000 description 1
- 108040007629 peroxidase activity proteins Proteins 0.000 description 1
- 150000002978 peroxides Chemical class 0.000 description 1
- 229920001983 poloxamer Polymers 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 229920005862 polyol Polymers 0.000 description 1
- 150000003077 polyols Chemical class 0.000 description 1
- 230000004481 post-translational protein modification Effects 0.000 description 1
- 108010066381 preproinsulin Proteins 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 239000013587 production medium Substances 0.000 description 1
- 230000001737 promoting effect Effects 0.000 description 1
- 230000000644 propagated effect Effects 0.000 description 1
- 230000000069 prophylactic effect Effects 0.000 description 1
- 108010087851 prorelaxin Proteins 0.000 description 1
- 230000001681 protective effect Effects 0.000 description 1
- 238000000159 protein binding assay Methods 0.000 description 1
- 229960000856 protein c Drugs 0.000 description 1
- 230000002797 proteolythic effect Effects 0.000 description 1
- 238000011002 quantification Methods 0.000 description 1
- 238000003127 radioimmunoassay Methods 0.000 description 1
- 230000002829 reductive effect Effects 0.000 description 1
- 230000001105 regulatory effect Effects 0.000 description 1
- 239000011347 resin Substances 0.000 description 1
- 229920005989 resin Polymers 0.000 description 1
- 238000004007 reversed phase HPLC Methods 0.000 description 1
- 238000005070 sampling Methods 0.000 description 1
- 229920006395 saturated elastomer Polymers 0.000 description 1
- 230000003248 secreting effect Effects 0.000 description 1
- 210000000717 sertoli cell Anatomy 0.000 description 1
- 125000005630 sialyl group Chemical group 0.000 description 1
- 239000000377 silicon dioxide Substances 0.000 description 1
- 238000011125 single therapy Methods 0.000 description 1
- 238000001542 size-exclusion chromatography Methods 0.000 description 1
- 239000001632 sodium acetate Substances 0.000 description 1
- 229960004249 sodium acetate Drugs 0.000 description 1
- 235000017281 sodium acetate Nutrition 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 238000012453 sprague-dawley rat model Methods 0.000 description 1
- 239000003381 stabilizer Substances 0.000 description 1
- 238000010186 staining Methods 0.000 description 1
- 230000004936 stimulating effect Effects 0.000 description 1
- 230000035882 stress Effects 0.000 description 1
- 230000001629 suppression Effects 0.000 description 1
- 230000004083 survival effect Effects 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 208000024891 symptom Diseases 0.000 description 1
- 230000009885 systemic effect Effects 0.000 description 1
- 125000000341 threoninyl group Chemical group [H]OC([H])(C([H])([H])[H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- 229960004072 thrombin Drugs 0.000 description 1
- 210000001685 thyroid gland Anatomy 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 238000001890 transfection Methods 0.000 description 1
- 239000012581 transferrin Substances 0.000 description 1
- 230000010474 transient expression Effects 0.000 description 1
- 238000013519 translation Methods 0.000 description 1
- QORWJWZARLRLPR-UHFFFAOYSA-H tricalcium bis(phosphate) Chemical compound [Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O QORWJWZARLRLPR-UHFFFAOYSA-H 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
- 239000003656 tris buffered saline Substances 0.000 description 1
- 230000006433 tumor necrosis factor production Effects 0.000 description 1
- 210000002700 urine Anatomy 0.000 description 1
- 229960005356 urokinase Drugs 0.000 description 1
- 210000003462 vein Anatomy 0.000 description 1
- 230000035899 viability Effects 0.000 description 1
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/005—Glycopeptides, glycoproteins
-
- 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
- C12N5/00—Undifferentiated human, animal or plant cells, e.g. cell lines; Tissues; Cultivation or maintenance thereof; Culture media therefor
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P29/00—Non-central analgesic, antipyretic or antiinflammatory agents, e.g. antirheumatic agents; Non-steroidal antiinflammatory drugs [NSAID]
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- 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
- C07K14/70503—Immunoglobulin superfamily
-
- 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
-
- 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
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K19/00—Hybrid peptides, i.e. peptides covalently bound to nucleic acids, or non-covalently bound protein-protein complexes
-
- 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
- C12N5/00—Undifferentiated human, animal or plant cells, e.g. cell lines; Tissues; Cultivation or maintenance thereof; Culture media therefor
- C12N5/0018—Culture media for cell or tissue culture
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
-
- 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
-
- 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
- C12N2500/00—Specific components of cell culture medium
- C12N2500/30—Organic components
- C12N2500/36—Lipids
-
- 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
- C12N2500/00—Specific components of cell culture medium
- C12N2500/60—Buffer, e.g. pH regulation, osmotic pressure
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Genetics & Genomics (AREA)
- General Health & Medical Sciences (AREA)
- Zoology (AREA)
- Biochemistry (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Immunology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Wood Science & Technology (AREA)
- Biotechnology (AREA)
- Biophysics (AREA)
- Cell Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biomedical Technology (AREA)
- Gastroenterology & Hepatology (AREA)
- Toxicology (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Engineering & Computer Science (AREA)
- Microbiology (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Pharmacology & Pharmacy (AREA)
- Pain & Pain Management (AREA)
- Rheumatology (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US08/469,348 US5705364A (en) | 1995-06-06 | 1995-06-06 | Mammalian cell culture process |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| OA10753A true OA10753A (en) | 2002-12-11 |
Family
ID=23863440
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| OA70153A OA10753A (en) | 1995-06-06 | 1997-12-05 | Process for controlling sialylation of proteins produced by mammalian cell culture |
Country Status (36)
| Country | Link |
|---|---|
| US (1) | US5705364A (fr) |
| EP (2) | EP1609853B2 (fr) |
| JP (2) | JPH11507523A (fr) |
| KR (1) | KR100496356B1 (fr) |
| CN (1) | CN1166772C (fr) |
| AR (2) | AR004940A1 (fr) |
| AT (2) | ATE302266T1 (fr) |
| AU (1) | AU717847B2 (fr) |
| BG (1) | BG63213B1 (fr) |
| BR (1) | BR9609150A (fr) |
| CA (1) | CA2220684C (fr) |
| CZ (1) | CZ293719B6 (fr) |
| DE (2) | DE69635076T3 (fr) |
| DK (2) | DK1609853T4 (fr) |
| EA (1) | EA001215B1 (fr) |
| ES (2) | ES2324046T5 (fr) |
| GE (1) | GEP20012519B (fr) |
| HK (2) | HK1017903A1 (fr) |
| HU (1) | HU226420B1 (fr) |
| IL (1) | IL122398A (fr) |
| IS (1) | IS2614B (fr) |
| MY (1) | MY113496A (fr) |
| NO (1) | NO322276B1 (fr) |
| NZ (1) | NZ310202A (fr) |
| OA (1) | OA10753A (fr) |
| PL (1) | PL185484B1 (fr) |
| PT (1) | PT1609853E (fr) |
| RO (1) | RO120267B1 (fr) |
| SA (1) | SA96170351B1 (fr) |
| SI (2) | SI1609853T2 (fr) |
| SK (1) | SK282658B6 (fr) |
| TR (1) | TR199701543T1 (fr) |
| TW (2) | TW426734B (fr) |
| UA (1) | UA47428C2 (fr) |
| WO (1) | WO1996039488A1 (fr) |
| ZA (1) | ZA964776B (fr) |
Families Citing this family (113)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE59010933D1 (de) | 1989-09-12 | 2003-05-08 | Hoffmann La Roche | TFN-bindende Proteine |
| US5705364A (en) † | 1995-06-06 | 1998-01-06 | Genentech, Inc. | Mammalian cell culture process |
| US6656466B1 (en) * | 1995-06-06 | 2003-12-02 | Genetech, Inc. | Human tumor necrosis factor—immunoglobulin(TNFR1-IgG1) chimera composition |
| JP4306813B2 (ja) | 1995-09-19 | 2009-08-05 | アスビオファーマ株式会社 | 動物細胞の新規培養方法 |
| KR20000010825A (ko) * | 1996-05-08 | 2000-02-25 | 프리돌린 클라우스너, 롤란드 비. 보레르 | 종양괴사인자 수용체-면역 글로불린 융합 단백질을 사용한 천식의 치료방법 |
| ES2252876T5 (es) * | 1997-12-03 | 2014-04-03 | Roche Diagnostics Gmbh | Proceso para preparar polipéptidos con glicolización adecuada |
| US6140445A (en) * | 1998-04-17 | 2000-10-31 | Crompton Corporation | Silane functional oligomer |
| US6528286B1 (en) * | 1998-05-29 | 2003-03-04 | Genentech, Inc. | Mammalian cell culture process for producing glycoproteins |
| EP1092037B1 (fr) * | 1998-05-29 | 2005-12-28 | Genentech, Inc. | Technique de culture de cellules en vue de la production de glycoproteines |
| TR200504220T2 (tr) * | 1998-12-17 | 2007-04-24 | Biogen Idec Ma Inc. | Aktif limfotoksin-beta reseptör imunoglobülin şimeAktif limfotoksin-beta reseptör imunoglobülin şimerik proteinlerinin yüksek düzey ifadesi ve saflaştrik proteinlerinin yüksek düzey ifadesi ve saflaştırılması için bir yöntem.ırılması için bir yöntem. |
| GB9828624D0 (en) * | 1998-12-23 | 1999-02-17 | Glaxo Group Ltd | Production of proteins |
| KR100475417B1 (ko) * | 1998-12-30 | 2005-07-18 | 씨제이 주식회사 | 시알산 함량이 높은 재조합 당단백질의 제조방법 |
| US7294481B1 (en) | 1999-01-05 | 2007-11-13 | Immunex Corporation | Method for producing recombinant proteins |
| ES2281342T3 (es) | 1999-04-26 | 2007-10-01 | Genentech, Inc. | Proceso de cultivo de celulas para la produccion de glicoproteinas. |
| US6261805B1 (en) * | 1999-07-15 | 2001-07-17 | Boyce Thompson Institute For Plant Research, Inc. | Sialyiation of N-linked glycoproteins in the baculovirus expression vector system |
| KR100394474B1 (ko) * | 1999-12-18 | 2003-08-09 | 동아제약 주식회사 | 동물세포에서 재조합 당단백질의 연속식 대량생산 방법 |
| ATE313554T1 (de) * | 2000-05-16 | 2006-01-15 | Lipoxen Technologies Ltd | Derivatisierung von proteinen in wässrigem lösungsmittel |
| WO2002002793A1 (fr) * | 2000-07-05 | 2002-01-10 | Japan As Represented By Secretary Of Osaka University | Processus de production de glycoproteine |
| US20030040095A1 (en) * | 2001-03-16 | 2003-02-27 | Achille Arini | Method for the production of pharmaceutically active recombinant proteins |
| WO2002101019A2 (fr) * | 2001-06-13 | 2002-12-19 | Genentech, Inc. | Procedes de mise en culture de cellules animales et production de polypeptides dans des cellules animales |
| WO2003083066A2 (fr) | 2002-03-27 | 2003-10-09 | Immunex Corporation | Procedes d'augmentation de la production de polypeptides |
| US20030190710A1 (en) * | 2002-03-28 | 2003-10-09 | Devries Ruth L. | Control of glycoforms in IgG |
| US7067279B1 (en) | 2002-08-23 | 2006-06-27 | Immunex Corporation | Cell culture performance with betaine |
| US6924124B1 (en) * | 2002-08-23 | 2005-08-02 | Immunex Corporation | Feeding strategies for cell culture |
| US6974681B1 (en) | 2002-08-23 | 2005-12-13 | Immunex Corporation | Cell culture performance with vanadate |
| RU2377253C2 (ru) * | 2002-12-02 | 2009-12-27 | Амген Фремонт,Инк. | Антитела, специфичные к фактору некроза опухолей, и их применение |
| MXPA05006522A (es) * | 2002-12-23 | 2006-02-17 | Bristol Myers Squibb Co | Mejora en la calidad de producto en procesos de cultivo en celulas de mamiferos para la produccion de proteina. |
| US7541164B2 (en) * | 2002-12-23 | 2009-06-02 | Bristol-Myers Squibb Company | Mammalian cell culture processes for protein production |
| AU2004234377A1 (en) * | 2003-04-25 | 2004-11-11 | Immunex Corporation | Inducers of recombinant protein expression |
| IN2014DN02483A (fr) | 2003-10-24 | 2015-05-15 | Selexis Sa | |
| EP1697414A2 (fr) * | 2003-12-23 | 2006-09-06 | Applied Research Systems ARS Holding N.V. | Procede de production de proteines de liaison au facteur de necrose tumorale |
| WO2005064002A1 (fr) * | 2003-12-31 | 2005-07-14 | Samyang Genex Corporation | Procede de production a grande echelle de metabolites secondaires dans une culture de cellules vegetales traitee avec un acide alcanoique ou un sel de celui-ci |
| JP4913604B2 (ja) * | 2004-02-13 | 2012-04-11 | グリコトープ ゲーエムベーハー | 高活性糖タンパク質−製造条件、及びその効率的製造方法 |
| US7300773B2 (en) * | 2004-08-27 | 2007-11-27 | Wyeth Research Ireland Limited | Production of TNFR-Ig |
| US7335491B2 (en) * | 2004-08-27 | 2008-02-26 | Wyeth Research Ireland Limited | Production of anti-abeta |
| US7294484B2 (en) * | 2004-08-27 | 2007-11-13 | Wyeth Research Ireland Limited | Production of polypeptides |
| CA2607663C (fr) * | 2005-05-19 | 2014-08-12 | Amgen Inc. | Compositions et procedes permettant d'accroitre la stabilite d'un anticorps |
| CA2610315A1 (fr) * | 2005-06-03 | 2006-12-07 | Biovitrum Ab (Publ) | Nouveau procede |
| KR100670105B1 (ko) | 2005-06-29 | 2007-01-17 | 주식회사 셀트리온 | 콩가수분해물의 저분자량 분획을 이용하여 시알산 함량이증가된 에리스로포이에틴을 생산하는 방법 및 그에 의하여생산된 시알산 함량이 증가된 에리스로포이에틴 |
| US8470318B2 (en) | 2005-11-07 | 2013-06-25 | The Rockefeller University | Polypeptides with enhanced anti-inflammatory and decreased cytotoxic properties and relating methods |
| WO2008057634A2 (fr) * | 2006-10-26 | 2008-05-15 | The Rockefeller University | Polypeptides ayant des propriétés antiinflammatoires accrues et cytotoxiques réduites et procédés associés |
| PT2253644E (pt) | 2005-12-20 | 2014-01-23 | Bristol Myers Squibb Co | Composições e métodos para a produção de uma composição |
| AR058568A1 (es) | 2005-12-20 | 2008-02-13 | Bristol Myers Squibb Co | Metodos para producir una composicion con moleculas ctla4-ig a partir de un medio de cultivo |
| US20070190057A1 (en) | 2006-01-23 | 2007-08-16 | Jian Wu | Methods for modulating mannose content of recombinant proteins |
| ES2502966T3 (es) * | 2006-01-26 | 2014-10-06 | Recopharma Ab | Composiciones y métodos para inhibir la adhesión viral |
| MX2008012843A (es) * | 2006-04-05 | 2009-01-19 | Univ Rockefeller | Polipeptidos con propiedades antiinflamatorias aumentadas y citotoxicas reducidas y metodos relacionados. |
| PT2495307T (pt) * | 2006-07-13 | 2018-05-10 | Wyeth Llc | Produção do fator ix de coagulação com padrão melhorado de glicosilação |
| US8911964B2 (en) | 2006-09-13 | 2014-12-16 | Abbvie Inc. | Fed-batch method of making human anti-TNF-alpha antibody |
| EP2527425A1 (fr) | 2006-09-13 | 2012-11-28 | Abbott Laboratories | Améliorations de culture cellulaire |
| US20080145893A1 (en) * | 2006-09-17 | 2008-06-19 | Excellegene Sa | Method for producing a recombinant protein at high specific productivity, high batch yield and high volumetric yield by means of transient transfection |
| WO2008069244A1 (fr) * | 2006-12-05 | 2008-06-12 | Kyowa Hakko Kogyo Co., Ltd. | Procédé de fabrication d'une composition de glycoprotéine |
| BRPI0810472A2 (pt) * | 2007-04-16 | 2014-11-11 | Momenta Pharmaceuticals Inc | Métodos relacionados à glicosilação da superfície celular |
| TW200902708A (en) | 2007-04-23 | 2009-01-16 | Wyeth Corp | Methods of protein production using anti-senescence compounds |
| US20090023186A1 (en) * | 2007-07-22 | 2009-01-22 | Excellgene Sa | Use of valproic acid for enhancing production of recombinant proteins in mammalian cells |
| ES2657055T3 (es) * | 2007-08-09 | 2018-03-01 | Wyeth Llc | Uso de perfusión para mejorar la producción de un cultivo de células alimentado por lotes en biorreactores |
| EP3760715B1 (fr) | 2008-03-06 | 2021-08-04 | Halozyme, Inc. | Production à large échelle d'hyaluronidase soluble |
| TWI395593B (zh) | 2008-03-06 | 2013-05-11 | Halozyme Inc | 可活化的基質降解酵素之活體內暫時性控制 |
| CA2720610C (fr) * | 2008-04-07 | 2016-08-23 | Bayer Healthcare Llc | Procedes de production recombinante de glycoproteines |
| AU2009240637A1 (en) | 2008-04-22 | 2009-10-29 | The Rockefeller University | Methods of identifying anti-inflammatory compounds |
| AU2009290563A1 (en) | 2008-09-15 | 2010-03-18 | Genentech, Inc. | Compositions and methods for regulating cell osmolarity |
| AU2009307737B2 (en) | 2008-10-20 | 2015-07-23 | Abbvie Inc. | Viral inactivation during purification of antibodies |
| SG10201702922VA (en) * | 2008-10-20 | 2017-06-29 | Abbvie Inc | Isolation and purification of antibodies using protein a affinity chromatography |
| RS58728B1 (sr) * | 2008-12-09 | 2019-06-28 | Halozyme Inc | Produženi rastvorljivi ph20 polipeptidi i njihove upotrebe |
| WO2010102262A1 (fr) * | 2009-03-06 | 2010-09-10 | Halozyme, Inc. | Mutants thermosensibles de métalloprotéase matricielle 1 et leurs utilisations |
| US9540426B2 (en) | 2009-10-06 | 2017-01-10 | Bristol-Myers Squibb Company | Mammalian cell culture processes for protein production |
| EP3202785B1 (fr) | 2009-10-26 | 2024-05-08 | F. Hoffmann-La Roche AG | Procédé de production d'immunoglobuline glycosylée |
| EP2501822B1 (fr) | 2009-11-17 | 2017-08-16 | E. R. Squibb & Sons, L.L.C. | Procédés pour une production améliorée de protéine |
| RU2012127383A (ru) * | 2009-12-02 | 2014-01-10 | Акселерон Фарма Инк. | Композиции и способы для увеличения времени полужизни fc-слитых белков в сыворотке |
| JP6021647B2 (ja) * | 2010-02-24 | 2016-11-09 | ザイムネックス エー／エス | 組み換えリソソームα−マンノシダーゼの生産および精製のための方法 |
| JPWO2012017925A1 (ja) | 2010-08-02 | 2013-10-03 | 協和発酵キリン株式会社 | 物質の製造方法 |
| EP2686423A4 (fr) | 2011-03-14 | 2015-01-28 | Nat Res Council Canada | Procédé de production virale dans des cellules |
| US9062106B2 (en) | 2011-04-27 | 2015-06-23 | Abbvie Inc. | Methods for controlling the galactosylation profile of recombinantly-expressed proteins |
| ES2560470T3 (es) | 2011-04-29 | 2016-02-19 | Biocon Research Limited | Un método para reducir la heterogeneidad de anticuerpos y un proceso de producción de dichos anticuerpos |
| WO2012170938A1 (fr) | 2011-06-08 | 2012-12-13 | Acceleron Pharma Inc. | Compositions et procédés pour augmenter la demi-vie sérique |
| US9150645B2 (en) | 2012-04-20 | 2015-10-06 | Abbvie, Inc. | Cell culture methods to reduce acidic species |
| US9067990B2 (en) | 2013-03-14 | 2015-06-30 | Abbvie, Inc. | Protein purification using displacement chromatography |
| US9181572B2 (en) | 2012-04-20 | 2015-11-10 | Abbvie, Inc. | Methods to modulate lysine variant distribution |
| US9249182B2 (en) | 2012-05-24 | 2016-02-02 | Abbvie, Inc. | Purification of antibodies using hydrophobic interaction chromatography |
| CN102839157A (zh) * | 2012-07-12 | 2012-12-26 | 扬州大学 | 稳定共表达hST3GalIV和β1-4GalT1的MDCK细胞系及构建方法和应用 |
| KR20150043523A (ko) | 2012-09-02 | 2015-04-22 | 애브비 인코포레이티드 | 단백질 불균일성의 제어 방법 |
| US9512214B2 (en) | 2012-09-02 | 2016-12-06 | Abbvie, Inc. | Methods to control protein heterogeneity |
| NO2760138T3 (fr) | 2012-10-01 | 2018-08-04 | ||
| US20140106405A1 (en) * | 2012-10-15 | 2014-04-17 | Bristol-Myers Squibb Company | Mammalian cell culture processes for protein production |
| EP2906683B1 (fr) | 2012-10-15 | 2017-05-31 | Bristol-Myers Squibb Company | Procédés de culture de cellules de mammifères en vue de la production de protéines |
| CA2905010A1 (fr) | 2013-03-12 | 2014-09-18 | Abbvie Inc. | Anticorps humains qui se lient au tnf-alpha et leurs procedes de preparation |
| US9499614B2 (en) | 2013-03-14 | 2016-11-22 | Abbvie Inc. | Methods for modulating protein glycosylation profiles of recombinant protein therapeutics using monosaccharides and oligosaccharides |
| US9017687B1 (en) | 2013-10-18 | 2015-04-28 | Abbvie, Inc. | Low acidic species compositions and methods for producing and using the same using displacement chromatography |
| WO2014159579A1 (fr) | 2013-03-14 | 2014-10-02 | Abbvie Inc. | Anticorps anti-tnfα ayant mutés et leurs procédés d'utilisation |
| US9217168B2 (en) | 2013-03-14 | 2015-12-22 | Momenta Pharmaceuticals, Inc. | Methods of cell culture |
| AR095196A1 (es) | 2013-03-15 | 2015-09-30 | Regeneron Pharma | Medio de cultivo celular libre de suero |
| CA2913687C (fr) | 2013-07-04 | 2022-12-13 | F. Hoffmann-La Roche Ag | Dosage immunologique a interference supprime et pour detecter des anticorps anti-medicament dans des echantillons de serum |
| CN105431454A (zh) | 2013-07-06 | 2016-03-23 | 卡迪拉保健有限公司 | 用于生产单克隆抗体的改进方法 |
| EP3052640A2 (fr) | 2013-10-04 | 2016-08-10 | AbbVie Inc. | Utilisation d'ions métaux pour la modulation des profils de glycosylation de protéines recombinantes |
| US8946395B1 (en) | 2013-10-18 | 2015-02-03 | Abbvie Inc. | Purification of proteins using hydrophobic interaction chromatography |
| US9085618B2 (en) | 2013-10-18 | 2015-07-21 | Abbvie, Inc. | Low acidic species compositions and methods for producing and using the same |
| US9181337B2 (en) | 2013-10-18 | 2015-11-10 | Abbvie, Inc. | Modulated lysine variant species compositions and methods for producing and using the same |
| WO2015073884A2 (fr) | 2013-11-15 | 2015-05-21 | Abbvie, Inc. | Compositions de protéines de liaison génétiquement glycomodifiées |
| BR112016017660B1 (pt) * | 2014-02-27 | 2022-04-19 | F. Hoffmann-La Roche Ag | Método para a produção de uma glicoproteína recombinante |
| JP6652334B2 (ja) | 2014-05-31 | 2020-02-19 | Ｊｃｒファーマ株式会社 | ウリジンとｎ−アセチル−ｄ−マンノサミンとを含有する培地 |
| AU2015270137A1 (en) * | 2014-06-03 | 2016-12-22 | Lupin Limited | Cell culture process for producing a protein |
| US20160130324A1 (en) | 2014-10-31 | 2016-05-12 | Shire Human Genetic Therapies, Inc. | C1 Inhibitor Fusion Proteins and Uses Thereof |
| KR102007930B1 (ko) | 2014-12-31 | 2019-08-06 | 주식회사 엘지화학 | 재조합 당단백질의 글리코실화 조절 방법 |
| TWI797060B (zh) | 2015-08-04 | 2023-04-01 | 美商再生元醫藥公司 | 補充牛磺酸之細胞培養基及用法 |
| MA43270A (fr) | 2015-11-19 | 2021-06-02 | Takeda Pharmaceuticals Co | Inhibiteur de la c1 estérase humaine recombinante et ses utilisations |
| WO2017114900A1 (fr) * | 2015-12-29 | 2017-07-06 | N.V. Nutricia | Préparation pour nourrissons fermentée comportant des oligosaccharides non digestibles |
| WO2019106097A1 (fr) * | 2017-11-30 | 2019-06-06 | F.Hoffmann-La Roche Ag | Procédé de culture de cellules de mammifère |
| US11634499B2 (en) | 2018-11-13 | 2023-04-25 | Janssen Biotech, Inc. | Control of trace metals during production of anti-CD38 antibodies |
| PE20221790A1 (es) | 2019-12-06 | 2022-11-25 | Regeneron Pharma | Composiciones de proteina anti-vegf y metodos para producir la misma |
| WO2022047108A1 (fr) | 2020-08-31 | 2022-03-03 | Regeneron Pharmaceuticals, Inc. | Stratégies d'alimentation d'asparagine pour améliorer la performance de culture cellulaire et atténuer des variants de séquence d'asparagine |
| CA3202197A1 (fr) | 2021-01-20 | 2022-07-28 | Reginald Smith | Procedes d'amelioration du titre proteique dans une culture cellulaire |
| AU2022359898A1 (en) | 2021-10-07 | 2024-03-21 | Regeneron Pharmaceuticals, Inc. | Ph meter calibration and correction |
| CN118076894A (zh) | 2021-10-07 | 2024-05-24 | 里珍纳龙药品有限公司 | pH建模和控制的系统及方法 |
| WO2023167857A1 (fr) | 2022-03-02 | 2023-09-07 | Regeneron Pharmaceuticals, Inc. | Procédés de culture cellulaire pour la production d'anticorps |
Family Cites Families (31)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US3926723A (en) | 1974-08-08 | 1975-12-16 | Massachusetts Inst Technology | Method of controllably releasing glucose to a cell culture medium |
| JPS5938488B2 (ja) | 1979-05-07 | 1984-09-17 | 株式会社東芝 | 空気調和機 |
| JPH0636751B2 (ja) * | 1982-06-21 | 1994-05-18 | ザ・ウエルカム・フアウンデ−シヨン・リミテツド | インタ−フエロンの改良製法 |
| US4560655A (en) | 1982-12-16 | 1985-12-24 | Immunex Corporation | Serum-free cell culture medium and process for making same |
| US4657866A (en) | 1982-12-21 | 1987-04-14 | Sudhir Kumar | Serum-free, synthetic, completely chemically defined tissue culture media |
| US4767704A (en) | 1983-10-07 | 1988-08-30 | Columbia University In The City Of New York | Protein-free culture medium |
| US4724206A (en) * | 1984-02-13 | 1988-02-09 | Damon Biotech, Inc. | Protein production using hypertonic media |
| GB8516415D0 (en) | 1985-06-28 | 1985-07-31 | Celltech Ltd | Culture of animal cells |
| JPH0639919B2 (ja) | 1985-08-29 | 1994-05-25 | トヨタ自動車株式会社 | 過給機付き内燃機関の異常判別装置 |
| GB8606386D0 (en) * | 1986-03-14 | 1986-04-23 | Celltech Ltd | Production of protein |
| US4927762A (en) | 1986-04-01 | 1990-05-22 | Cell Enterprises, Inc. | Cell culture medium with antioxidant |
| WO1988001643A1 (fr) | 1986-08-29 | 1988-03-10 | Endotronics, Inc. | Procede de culture cellulaire |
| JPH01257492A (ja) * | 1987-03-05 | 1989-10-13 | Green Cross Corp:The | 異種蛋白質の生産増強方法 |
| IL87737A (en) * | 1987-09-11 | 1993-08-18 | Genentech Inc | Method for culturing polypeptide factor dependent vertebrate recombinant cells |
| JPH066054B2 (ja) | 1987-10-15 | 1994-01-26 | 帝人株式会社 | 動物細胞の培養方法 |
| CA1312030C (fr) * | 1987-11-18 | 1992-12-29 | Brian Maiorella | Methode pour accroitre le titre d'anticorps |
| US5151359A (en) * | 1988-05-19 | 1992-09-29 | Mitsui Toatsu Chemicals Incorporated | Method for producing of human tissue type plasminogen activator |
| EP0435911B1 (fr) | 1988-09-23 | 1996-03-13 | Cetus Oncology Corporation | Milieu de culture de cellules pour l'amelioration de la croissance des cellules, de la longivite de la culture et de l'expression du produit |
| KR0132666B1 (en) * | 1989-03-14 | 1998-04-14 | Hitachi Kk | Method for controlling cultivation conditions for animal cells |
| JPH0396383A (ja) | 1989-09-08 | 1991-04-22 | Riso Kagaku Corp | 画像形成装置 |
| DE59010933D1 (de) | 1989-09-12 | 2003-05-08 | Hoffmann La Roche | TFN-bindende Proteine |
| US5096816A (en) * | 1990-06-05 | 1992-03-17 | Cetus Corporation | In vitro management of ammonia's effect on glycosylation of cell products through pH control |
| US5122469A (en) * | 1990-10-03 | 1992-06-16 | Genentech, Inc. | Method for culturing Chinese hamster ovary cells to improve production of recombinant proteins |
| GB9022545D0 (en) * | 1990-10-17 | 1990-11-28 | Wellcome Found | Culture medium |
| GB2251249B (en) * | 1990-12-28 | 1995-06-21 | Mogam Biotech Res Inst | High-density medium for animal cell culture |
| WO1993010260A1 (fr) * | 1991-11-21 | 1993-05-27 | The Board Of Trustees Of The Leland Stanford Junior University | Utilisation de la neuraminidase extracellulaire pour lutter contre la degradation d'oligosaccharides de la glycoproteine |
| US5447851B1 (en) * | 1992-04-02 | 1999-07-06 | Univ Texas System Board Of | Dna encoding a chimeric polypeptide comprising the extracellular domain of tnf receptor fused to igg vectors and host cells |
| CA2123593C (fr) * | 1992-09-15 | 2000-03-14 | Craig A. Smith | Methode de traitement de l'inflammation dependante du tnf a l'aide d'antagonistes du facteur de necrose tumorale |
| JP3523293B2 (ja) † | 1993-07-19 | 2004-04-26 | 住友製薬株式会社 | インターフェロンの産生増強法 |
| US5705364A (en) † | 1995-06-06 | 1998-01-06 | Genentech, Inc. | Mammalian cell culture process |
| JP5515221B2 (ja) † | 2008-01-28 | 2014-06-11 | 日油株式会社 | ポリオキシエチレンソルビタン脂肪酸エステルの製造方法 |
-
1995
- 1995-06-06 US US08/469,348 patent/US5705364A/en not_active Expired - Lifetime
-
1996
- 1996-06-05 TW TW085106712A patent/TW426734B/zh not_active IP Right Cessation
- 1996-06-05 TW TW089111534A patent/TW516962B/zh not_active IP Right Cessation
- 1996-06-06 JP JP9501638A patent/JPH11507523A/ja not_active Withdrawn
- 1996-06-06 EP EP05017434.1A patent/EP1609853B2/fr not_active Expired - Lifetime
- 1996-06-06 WO PCT/US1996/009284 patent/WO1996039488A1/fr active IP Right Grant
- 1996-06-06 SI SI9630767T patent/SI1609853T2/sl unknown
- 1996-06-06 IL IL12239896A patent/IL122398A/en not_active IP Right Cessation
- 1996-06-06 CA CA002220684A patent/CA2220684C/fr not_active Expired - Lifetime
- 1996-06-06 AR ARP960103001A patent/AR004940A1/es active IP Right Grant
- 1996-06-06 DK DK05017434.1T patent/DK1609853T4/da active
- 1996-06-06 ZA ZA9604776A patent/ZA964776B/xx unknown
- 1996-06-06 EA EA199700364A patent/EA001215B1/ru not_active IP Right Cessation
- 1996-06-06 UA UA97125856A patent/UA47428C2/uk unknown
- 1996-06-06 PL PL96323737A patent/PL185484B1/pl unknown
- 1996-06-06 HU HU9900920A patent/HU226420B1/hu unknown
- 1996-06-06 MY MYPI96002265A patent/MY113496A/en unknown
- 1996-06-06 ES ES05017434T patent/ES2324046T5/es not_active Expired - Lifetime
- 1996-06-06 PT PT05017434T patent/PT1609853E/pt unknown
- 1996-06-06 NZ NZ310202A patent/NZ310202A/en not_active IP Right Cessation
- 1996-06-06 AT AT96918251T patent/ATE302266T1/de active
- 1996-06-06 EP EP96918251A patent/EP0832189B2/fr not_active Expired - Lifetime
- 1996-06-06 RO RO97-02262A patent/RO120267B1/ro unknown
- 1996-06-06 TR TR97/01543T patent/TR199701543T1/xx unknown
- 1996-06-06 KR KR1019970708954A patent/KR100496356B1/ko not_active IP Right Cessation
- 1996-06-06 ES ES96918251T patent/ES2248812T5/es not_active Expired - Lifetime
- 1996-06-06 DE DE69635076T patent/DE69635076T3/de not_active Expired - Lifetime
- 1996-06-06 CZ CZ19973909A patent/CZ293719B6/cs not_active IP Right Cessation
- 1996-06-06 AT AT05017434T patent/ATE425245T2/de active
- 1996-06-06 BR BR9609150A patent/BR9609150A/pt not_active Application Discontinuation
- 1996-06-06 DK DK96918251T patent/DK0832189T4/da active
- 1996-06-06 SI SI9630715T patent/SI0832189T2/sl unknown
- 1996-06-06 AU AU60952/96A patent/AU717847B2/en not_active Expired
- 1996-06-06 DE DE69637867T patent/DE69637867D1/de not_active Expired - Lifetime
- 1996-06-06 CN CNB961944498A patent/CN1166772C/zh not_active Expired - Lifetime
- 1996-06-06 SK SK1670-97A patent/SK282658B6/sk not_active IP Right Cessation
- 1996-06-06 GE GEAP19964011A patent/GEP20012519B/en unknown
- 1996-10-07 SA SA96170351A patent/SA96170351B1/ar unknown
-
1997
- 1997-12-03 IS IS4626A patent/IS2614B/is unknown
- 1997-12-03 BG BG102101A patent/BG63213B1/bg unknown
- 1997-12-05 NO NO19975674A patent/NO322276B1/no not_active IP Right Cessation
- 1997-12-05 OA OA70153A patent/OA10753A/en unknown
-
1998
- 1998-02-12 AR ARP980100640A patent/AR011439A2/es unknown
- 1998-12-23 HK HK98114966A patent/HK1017903A1/xx not_active IP Right Cessation
-
2006
- 2006-06-28 HK HK06107347.9A patent/HK1087151A1/xx not_active IP Right Cessation
-
2007
- 2007-02-28 JP JP2007050848A patent/JP4348376B2/ja not_active Expired - Lifetime
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| OA10753A (en) | Process for controlling sialylation of proteins produced by mammalian cell culture | |
| US5721121A (en) | Mammalian cell culture process for producing a tumor necrosis factor receptor immunoglobulin chimeric protein | |
| US6656466B1 (en) | Human tumor necrosis factor—immunoglobulin(TNFR1-IgG1) chimera composition | |
| US6528286B1 (en) | Mammalian cell culture process for producing glycoproteins | |
| JP5881755B2 (ja) | 細胞培養における低温および低ｐＨの使用 | |
| EP1092037B1 (fr) | Technique de culture de cellules en vue de la production de glycoproteines | |
| US6693181B2 (en) | Protein secretion | |
| MXPA97009452A (en) | Process to control the sialilation of proteins produced by cultivation of mamife cells |