IL118201A - Preparation comprising a protein with human erythropoietin activity which is free of serum and non-recombinant mammalian protein and process for the preparation thereof - Google Patents

Preparation comprising a protein with human erythropoietin activity which is free of serum and non-recombinant mammalian protein and process for the preparation thereof

Info

Publication number: IL118201A
Authority: IL; Israel
Prior art keywords: host cell; protein; chromatography; preparation; epo
Prior art date: 1995-05-11

Application number

IL11820196A

Other languages

English (en)

Other versions

IL118201A0 (en

Original Assignee

Roche Diagnostics Gmbh

Priority date (The priority date 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 date listed.)

1995-05-11

Filing date

1996-05-09

Publication date

2004-12-15

1996-05-09 Application filed by Roche Diagnostics Gmbh filed Critical Roche Diagnostics Gmbh

1996-09-12 Publication of IL118201A0 publication Critical patent/IL118201A0/xx

2003-08-28 Priority to IL15764403A priority Critical patent/IL157644A0/xx

2004-12-15 Publication of IL118201A publication Critical patent/IL118201A/en

Links

108090000623 proteins and genes Proteins 0.000 title claims abstract description 74
102000004169 proteins and genes Human genes 0.000 title claims abstract description 70
230000000694 effects Effects 0.000 title claims abstract description 10
238000000034 method Methods 0.000 title claims description 33
238000002360 preparation method Methods 0.000 title claims description 27
230000008569 process Effects 0.000 title claims description 16
210000002966 serum Anatomy 0.000 title claims description 9
101000987586 Homo sapiens Eosinophil peroxidase Proteins 0.000 title claims description 7
102000044890 human EPO Human genes 0.000 title claims description 7
101000920686 Homo sapiens Erythropoietin Proteins 0.000 title claims description 6
102000003951 Erythropoietin Human genes 0.000 claims abstract description 64
108090000394 Erythropoietin Proteins 0.000 claims abstract description 64
229940105423 erythropoietin Drugs 0.000 claims abstract description 64
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 claims abstract description 64
210000004027 cell Anatomy 0.000 claims description 57
KFZMGEQAYNKOFK-UHFFFAOYSA-N Isopropanol Chemical compound CC(C)O KFZMGEQAYNKOFK-UHFFFAOYSA-N 0.000 claims description 42
238000004587 chromatography analysis Methods 0.000 claims description 33
108020004414 DNA Proteins 0.000 claims description 24
230000002209 hydrophobic effect Effects 0.000 claims description 14
238000010828 elution Methods 0.000 claims description 11
238000004519 manufacturing process Methods 0.000 claims description 6
230000007935 neutral effect Effects 0.000 claims description 6
238000001042 affinity chromatography Methods 0.000 claims description 5
238000004366 reverse phase liquid chromatography Methods 0.000 claims description 5
239000012679 serum free medium Substances 0.000 claims description 5
238000000855 fermentation Methods 0.000 claims description 4
230000004151 fermentation Effects 0.000 claims description 4
238000011068 loading method Methods 0.000 claims description 4
LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 claims description 3
238000005571 anion exchange chromatography Methods 0.000 claims description 3
238000011210 chromatographic step Methods 0.000 claims description 2
230000004069 differentiation Effects 0.000 claims description 2
210000003013 erythroid precursor cell Anatomy 0.000 claims description 2
239000006228 supernatant Substances 0.000 claims description 2
230000001225 therapeutic effect Effects 0.000 abstract description 5
235000018102 proteins Nutrition 0.000 description 53
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 20
239000006167 equilibration buffer Substances 0.000 description 18
238000000746 purification Methods 0.000 description 14
239000000463 material Substances 0.000 description 13
239000011534 wash buffer Substances 0.000 description 13
HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 12
UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 10
229920002684 Sepharose Polymers 0.000 description 10
DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 10
239000001110 calcium chloride Substances 0.000 description 10
235000011148 calcium chloride Nutrition 0.000 description 10
229910001628 calcium chloride Inorganic materials 0.000 description 10
239000000975 dye Substances 0.000 description 10
239000012149 elution buffer Substances 0.000 description 10
239000011780 sodium chloride Substances 0.000 description 10
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 9
WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 9
101150002621 EPO gene Proteins 0.000 description 9
239000000872 buffer Substances 0.000 description 8
229910052588 hydroxylapatite Inorganic materials 0.000 description 8
239000011159 matrix material Substances 0.000 description 8
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 8
238000000926 separation method Methods 0.000 description 8
229910019142 PO4 Inorganic materials 0.000 description 7
239000010452 phosphate Substances 0.000 description 7
QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 6
239000002609 medium Substances 0.000 description 6
239000011734 sodium Substances 0.000 description 6
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241000283690 Bos taurus Species 0.000 description 5
210000004978 chinese hamster ovary cell Anatomy 0.000 description 5
238000004128 high performance liquid chromatography Methods 0.000 description 5
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238000001914 filtration Methods 0.000 description 4
JYGXADMDTFJGBT-VWUMJDOOSA-N hydrocortisone Chemical compound O=C1CC[C@]2(C)[C@H]3[C@@H](O)C[C@](C)([C@@](CC4)(O)C(=O)CO)[C@@H]4[C@@H]3CCC2=C1 JYGXADMDTFJGBT-VWUMJDOOSA-N 0.000 description 4
238000004007 reversed phase HPLC Methods 0.000 description 4
150000003839 salts Chemical class 0.000 description 4
229920002271 DEAE-Sepharose Polymers 0.000 description 3
LYCAIKOWRPUZTN-UHFFFAOYSA-N Ethylene glycol Chemical compound OCCO LYCAIKOWRPUZTN-UHFFFAOYSA-N 0.000 description 3
PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
244000309466 calf Species 0.000 description 3
239000003795 chemical substances by application Substances 0.000 description 3
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238000012545 processing Methods 0.000 description 3
MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 2
JYEUMXHLPRZUAT-UHFFFAOYSA-N 1,2,3-triazine Chemical compound C1=CN=NN=C1 JYEUMXHLPRZUAT-UHFFFAOYSA-N 0.000 description 2
QTBSBXVTEAMEQO-UHFFFAOYSA-M Acetate Chemical compound CC([O-])=O QTBSBXVTEAMEQO-UHFFFAOYSA-M 0.000 description 2
229920000936 Agarose Polymers 0.000 description 2
DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 2
241000894006 Bacteria Species 0.000 description 2
108091003079 Bovine Serum Albumin Proteins 0.000 description 2
241000588724 Escherichia coli Species 0.000 description 2
108091029865 Exogenous DNA Proteins 0.000 description 2
DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 2
CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 2
ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 2
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MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 2
UIIMBOGNXHQVGW-DEQYMQKBSA-M Sodium bicarbonate-14C Chemical compound [Na+].O[14C]([O-])=O UIIMBOGNXHQVGW-DEQYMQKBSA-M 0.000 description 2
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125000000217 alkyl group Chemical group 0.000 description 2
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235000003704 aspartic acid Nutrition 0.000 description 2
239000011324 bead Substances 0.000 description 2
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 2
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GHWVXCQZPNWFRO-UHFFFAOYSA-N butane-2,3-diamine Chemical compound CC(N)C(C)N GHWVXCQZPNWFRO-UHFFFAOYSA-N 0.000 description 2
125000000484 butyl group Chemical group [H]C([*])([H])C([H])([H])C([H])([H])C([H])([H])[H] 0.000 description 2
BVTBRVFYZUCAKH-UHFFFAOYSA-L disodium selenite Chemical compound [Na+].[Na+].[O-][Se]([O-])=O BVTBRVFYZUCAKH-UHFFFAOYSA-L 0.000 description 2
238000011067 equilibration Methods 0.000 description 2
210000003743 erythrocyte Anatomy 0.000 description 2
238000001641 gel filtration chromatography Methods 0.000 description 2
229960002743 glutamine Drugs 0.000 description 2
230000006801 homologous recombination Effects 0.000 description 2
238000002744 homologous recombination Methods 0.000 description 2
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NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 description 2
230000003993 interaction Effects 0.000 description 2
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210000004962 mammalian cell Anatomy 0.000 description 2
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238000001742 protein purification Methods 0.000 description 2
235000004400 serine Nutrition 0.000 description 2
235000015921 sodium selenite Nutrition 0.000 description 2
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239000000243 solution Substances 0.000 description 2
239000002904 solvent Substances 0.000 description 2
LWIHDJKSTIGBAC-UHFFFAOYSA-K tripotassium phosphate Chemical compound [K+].[K+].[K+].[O-]P([O-])([O-])=O LWIHDJKSTIGBAC-UHFFFAOYSA-K 0.000 description 2
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GUPXYSSGJWIURR-UHFFFAOYSA-N 3-octoxypropane-1,2-diol Chemical compound CCCCCCCCOCC(O)CO GUPXYSSGJWIURR-UHFFFAOYSA-N 0.000 description 1
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239000006144 Dulbecco’s modiﬁed Eagle's medium Substances 0.000 description 1
238000002965 ELISA Methods 0.000 description 1
108010010803 Gelatin Proteins 0.000 description 1
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102000003886 Glycoproteins Human genes 0.000 description 1
108090000288 Glycoproteins Proteins 0.000 description 1
101100333654 Homo sapiens EPO gene Proteins 0.000 description 1
229930182816 L-glutamine Natural products 0.000 description 1
241001494479 Pecora Species 0.000 description 1
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108091005804 Peptidases Proteins 0.000 description 1
239000004365 Protease Substances 0.000 description 1
VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 1
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ZMZDMBWJUHKJPS-UHFFFAOYSA-M Thiocyanate anion Chemical compound [S-]C#N ZMZDMBWJUHKJPS-UHFFFAOYSA-M 0.000 description 1
102000004338 Transferrin Human genes 0.000 description 1
108090000901 Transferrin Proteins 0.000 description 1
102000002070 Transferrins Human genes 0.000 description 1
108010015865 Transferrins Proteins 0.000 description 1
241000700605 Viruses Species 0.000 description 1
239000003929 acidic solution Substances 0.000 description 1
230000009471 action Effects 0.000 description 1
230000004913 activation Effects 0.000 description 1
239000000654 additive Substances 0.000 description 1
GZCGUPFRVQAUEE-SLPGGIOYSA-N aldehydo-D-glucose Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C=O GZCGUPFRVQAUEE-SLPGGIOYSA-N 0.000 description 1
235000001014 amino acid Nutrition 0.000 description 1
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210000004102 animal cell Anatomy 0.000 description 1
239000012062 aqueous buffer Substances 0.000 description 1
239000007864 aqueous solution Substances 0.000 description 1
238000010923 batch production Methods 0.000 description 1
230000015572 biosynthetic process Effects 0.000 description 1
210000004369 blood Anatomy 0.000 description 1
239000008280 blood Substances 0.000 description 1
IXIBAKNTJSCKJM-BUBXBXGNSA-N bovine insulin 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)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)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(C)C)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 IXIBAKNTJSCKJM-BUBXBXGNSA-N 0.000 description 1
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229910000389 calcium phosphate Inorganic materials 0.000 description 1
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238000004113 cell culture Methods 0.000 description 1
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235000019322 gelatine Nutrition 0.000 description 1
235000011852 gelatine desserts Nutrition 0.000 description 1
229960001031 glucose Drugs 0.000 description 1
239000008103 glucose Substances 0.000 description 1
ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
150000004676 glycans Chemical class 0.000 description 1
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229960004198 guanidine Drugs 0.000 description 1
PJJJBBJSCAKJQF-UHFFFAOYSA-N guanidinium chloride Chemical compound [Cl-].NC(N)=[NH2+] PJJJBBJSCAKJQF-UHFFFAOYSA-N 0.000 description 1
238000003306 harvesting Methods 0.000 description 1
XMBWDFGMSWQBCA-UHFFFAOYSA-N hydrogen iodide Chemical compound I XMBWDFGMSWQBCA-UHFFFAOYSA-N 0.000 description 1
ZMZDMBWJUHKJPS-UHFFFAOYSA-N hydrogen thiocyanate Natural products SC#N ZMZDMBWJUHKJPS-UHFFFAOYSA-N 0.000 description 1
230000003053 immunization Effects 0.000 description 1
229940125396 insulin Drugs 0.000 description 1
239000004026 insulin derivative Substances 0.000 description 1
230000003834 intracellular effect Effects 0.000 description 1
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BAUYGSIQEAFULO-UHFFFAOYSA-L iron(2+) sulfate (anhydrous) Chemical compound [Fe+2].[O-]S([O-])(=O)=O BAUYGSIQEAFULO-UHFFFAOYSA-L 0.000 description 1
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238000002955 isolation Methods 0.000 description 1
210000003734 kidney Anatomy 0.000 description 1
210000003292 kidney cell Anatomy 0.000 description 1
210000004185 liver Anatomy 0.000 description 1
210000002751 lymph Anatomy 0.000 description 1
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VLTRZXGMWDSKGL-UHFFFAOYSA-M perchlorate Inorganic materials [O-]Cl(=O)(=O)=O VLTRZXGMWDSKGL-UHFFFAOYSA-M 0.000 description 1
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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
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Classifications

- 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
- C07K14/475—Growth factors; Growth regulators
- C07K14/505—Erythropoietin [EPO]

Landscapes

Chemical & Material Sciences (AREA)
Health & Medical Sciences (AREA)
Life Sciences & Earth Sciences (AREA)
Organic Chemistry (AREA)
General Health & Medical Sciences (AREA)
Gastroenterology & Hepatology (AREA)
Biochemistry (AREA)
Biophysics (AREA)
Zoology (AREA)
Genetics & Genomics (AREA)
Medicinal Chemistry (AREA)
Molecular Biology (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Toxicology (AREA)
Peptides Or Proteins (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)

IL11820196A 1995-05-11 1996-05-09 Preparation comprising a protein with human erythropoietin activity which is free of serum and non-recombinant mammalian protein and process for the preparation thereof IL118201A (en)

Priority Applications (1)

Application Number	Priority Date	Filing Date	Title
IL15764403A IL157644A0 (en)	1995-05-11	2003-08-28	Method for the purification of a protein preparation with erythropoietin activity

Applications Claiming Priority (2)

Application Number	Priority Date	Filing Date	Title
EP95107165		1995-05-11
DE19522461		1995-06-21

Publications (2)

Publication Number	Publication Date
IL118201A0 IL118201A0 (en)	1996-09-12
IL118201A true IL118201A (en)	2004-12-15

Family

ID=26016131

Family Applications (2)

Application Number	Title	Priority Date	Filing Date
IL11820196A IL118201A (en)	1995-05-11	1996-05-09	Preparation comprising a protein with human erythropoietin activity which is free of serum and non-recombinant mammalian protein and process for the preparation thereof
IL15764403A IL157644A0 (en)	1995-05-11	2003-08-28	Method for the purification of a protein preparation with erythropoietin activity

Family Applications After (1)

Application Number	Title	Priority Date	Filing Date
IL15764403A IL157644A0 (en)	1995-05-11	2003-08-28	Method for the purification of a protein preparation with erythropoietin activity

Country Status (12)

Country	Link
US (2)	US6399333B1 (fr)
EP (2)	EP1394179B1 (fr)
JP (1)	JP3061200B2 (fr)
AT (2)	ATE258189T1 (fr)
AU (1)	AU5817496A (fr)
CA (1)	CA2220515C (fr)
DE (2)	DE59611371D1 (fr)
DK (2)	DK0830376T3 (fr)
ES (2)	ES2268232T3 (fr)
IL (2)	IL118201A (fr)
PT (2)	PT1394179E (fr)
WO (1)	WO1996035718A1 (fr)

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BR9905868A (pt)	1998-11-06	2001-01-23	Bio Sidus S A	Procedimento de cultivo massivo de células de mamìfero para a obtenção de eritropoetina humana, recombinante e a eritropoetina humana recombinante obtida com tal procedimento
BR9905867A (pt) *	1998-11-06	2001-01-23	Bio Sidus S A	Linhagem celular produtora de eritropoietina humana recombinante e a eritropoietina humana recombinante produzida por esta célula
JO2291B1 (en)	1999-07-02	2005-09-12	اف . هوفمان لاروش ايه جي	Erythropoietin derivatives
AU2002233230B2 (en)	2000-12-20	2007-02-01	F. Hoffmann-La Roche Ag	Erythropoietin conjugates
CN1596310A (zh) *	2001-11-28	2005-03-16	桑多斯有限公司	产生重组多肽的方法
ATE363541T1 (de) *	2002-03-26	2007-06-15	Lek Tovarna Farmacevtskih	Verfahren für die herstellung eines gewünschten profils von erythropoietin glyko-isoformen
DE60228460D1 (de) *	2002-12-13	2008-10-02	Bioceuticals Arzneimittel Ag	Verfahren zur Herstellung und Reinigung von Erythropoietin
US20050019914A1 (en) *	2003-07-24	2005-01-27	Aventis Pharma Deutschland Gmbh	Perfusion process for producing erythropoietin
EP1670821A4 (fr) *	2003-10-09	2006-11-29	Daewoong Co Ltd	Procede de purification de la thrombopoietine humaine a teneur en acide sialique elevee
DE102004027816A1 (de) *	2004-06-08	2006-01-05	Bioceuticals Arzneimittel Ag	Verfahren zur Reinigung von Erythropoietin
US7598356B2 (en) *	2004-07-08	2009-10-06	Board of Regents of the University of Nebraska by and on behalf of the University of Nebraska Medical Center	Method for purifying a protein of the cystine-knot superfamily
DE602004013847D1 (de) *	2004-11-09	2008-06-26	Usv Ltd	Neues verfahren zur aufreinigung von humanem wachstumshormon
ES2509872T3 (es) *	2005-03-03	2014-10-20	Allergan, Inc.	Procedimientos para obtener una toxina clostrídica
EP2495308A1 (fr)	2005-12-08	2012-09-05	Amgen Inc.	Production améliorée de glycoprotéines au moyen de manganèse
PL2054074T3 (pl)	2006-08-04	2015-03-31	Prolong Pharmaceuticals Llc	Zmodyfikowana erytropoetyna
EP2089424B1 (fr) *	2006-12-06	2015-07-01	JCR PHARMACEUTICALS Co., LTD.	Procédé de production d'érythropoïétine humaine
KR100988706B1 (ko)	2007-03-07	2010-10-18	한미홀딩스 주식회사	재조합 에리트로포이에틴의 신규한 정제방법
CL2008002053A1 (es)	2007-07-17	2009-05-22	Hoffmann La Roche	Metodo para la purificacion de una eritropoyetina monopeguilada (epompeg) que consiste en proporcionar una solucion que contiene eritropoyetina mono, poli y no peguilada y hacerla pasar por dos pasos de cromatografia de intercambio cationico y metodo para producir epo mpeg que incluye metodo de purificacion.
AR067536A1 (es) *	2007-07-17	2009-10-14	Hoffmann La Roche	Metodo para obtener una eritropoyetina mono-pegilada en una forma sustancialmente homogenea
KR100900033B1 (ko)	2007-11-21	2009-06-01	한국생명공학연구원	인간 에리스로포이에틴의 정제방법
MX344166B (es)	2008-02-08	2016-12-07	Ambrx Inc	Leptina-polipeptidos modificados y sus usos.
DE102008002210A1 (de) *	2008-06-04	2009-12-10	Evonik Degussa Gmbh	Verfahren zur fermentativen Herstellung von Erythropoietin
DE102008002209A1 (de)	2008-06-04	2009-12-10	Evonik Degussa Gmbh	Verfahren zur Aufreinigung von Erythropoietin
CN102164954B (zh)	2008-09-23	2018-04-06	弗·哈夫曼-拉罗切有限公司	促红细胞生成素的纯化
BR122012024318A2 (pt)	2008-09-26	2019-07-30	Ambrx, Inc.	Polipeptídeos modificados de eritropoetina animal e seus usos
DE102008054716A1 (de)	2008-12-16	2010-06-17	Evonik Degussa Gmbh	Inprozesskontrolle in einem Verfahren zur Herstellung von EPO
US20120177640A1 (en)	2009-07-24	2012-07-12	Josef Burg	Optimizing the production of antibodies
EA022396B1 (ru)	2009-09-23	2015-12-30	Ратиофарм Гмбх	Способ очистки рекомбинантного эритропоэтина человека (epo), эритропоэтин, очищенный данным способом, и фармацевтические композиции, содержащие такой эритропоэтин
KR101443257B1 (ko) *	2011-10-18	2014-09-19	주식회사 종근당	낮은 등전점을 갖는 에리스로포이에틴 유사체의 정제방법
US10066001B2 (en)	2013-03-15	2018-09-04	Apotex Inc.	Enhanced liquid formulation stability of erythropoietin alpha through purification processing
WO2016116966A1 (fr) *	2015-01-22	2016-07-28	Jcr Pharmaceuticals Co., Ltd.	Procédé de purification d'une alpha-galactosidase a recombinante humaine à partir de matériel contenant des protéines contaminantes des cellules hôtes
DK3613486T3 (da) *	2018-08-24	2021-01-04	Uga Biopharma Gmbh	Metode og anlæg til rengøring af epo og/eller et epo-derivat

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IL79176A (en) *	1985-06-20	1992-06-21	Kirin Amgen Inc	Process for the recovery of erythropoietin from a fluid
US4954437A (en) *	1986-09-15	1990-09-04	Integrated Genetics, Inc.	Cell encoding recombinant human erythropoietin
AU4104889A (en)	1988-09-07	1990-03-15	Bioclones (Pty) Ltd	Purification of erythropoietin
DE4115722A1 (de) *	1991-05-14	1992-11-19	Boehringer Mannheim Gmbh	Serumfreies medium zur kultivierung von saeugerzellen

1996
- 1996-05-09 IL IL11820196A patent/IL118201A/en not_active IP Right Cessation
- 1996-05-10 AT AT96919753T patent/ATE258189T1/de active
- 1996-05-10 ES ES03016548T patent/ES2268232T3/es not_active Expired - Lifetime
- 1996-05-10 ES ES96919753T patent/ES2211961T3/es not_active Expired - Lifetime
- 1996-05-10 EP EP03016548A patent/EP1394179B1/fr not_active Expired - Lifetime
- 1996-05-10 US US08/945,802 patent/US6399333B1/en not_active Expired - Lifetime
- 1996-05-10 WO PCT/EP1996/001988 patent/WO1996035718A1/fr not_active Ceased
- 1996-05-10 DK DK96919753T patent/DK0830376T3/da active
- 1996-05-10 EP EP96919753A patent/EP0830376B1/fr not_active Expired - Lifetime
- 1996-05-10 CA CA002220515A patent/CA2220515C/fr not_active Expired - Lifetime
- 1996-05-10 AT AT03016548T patent/ATE334146T1/de active
- 1996-05-10 DE DE59611371T patent/DE59611371D1/de not_active Expired - Lifetime
- 1996-05-10 PT PT03016548T patent/PT1394179E/pt unknown
- 1996-05-10 AU AU58174/96A patent/AU5817496A/en not_active Abandoned
- 1996-05-10 PT PT96919753T patent/PT830376E/pt unknown
- 1996-05-10 DE DE59610898T patent/DE59610898D1/de not_active Expired - Lifetime
- 1996-05-10 DK DK03016548T patent/DK1394179T3/da active
- 1996-05-10 JP JP8533775A patent/JP3061200B2/ja not_active Expired - Lifetime
2002
- 2002-02-07 US US10/067,235 patent/US6471500B1/en not_active Expired - Lifetime
2003
- 2003-08-28 IL IL15764403A patent/IL157644A0/xx unknown

Also Published As

Publication number	Publication date
IL118201A0 (en)	1996-09-12
DK0830376T3 (da)	2004-05-24
PT1394179E (pt)	2006-11-30
DE59610898D1 (de)	2004-02-26
WO1996035718A1 (fr)	1996-11-14
JP3061200B2 (ja)	2000-07-10
JPH10506924A (ja)	1998-07-07
ATE334146T1 (de)	2006-08-15
ATE258189T1 (de)	2004-02-15
PT830376E (pt)	2004-05-31
CA2220515C (fr)	2003-07-22
EP1394179A1 (fr)	2004-03-03
EP0830376B1 (fr)	2004-01-21
US6471500B1 (en)	2002-10-29
ES2211961T3 (es)	2004-07-16
AU5817496A (en)	1996-11-29
IL157644A0 (en)	2004-03-28
DK1394179T3 (da)	2006-11-20
US20020146771A1 (en)	2002-10-10
EP1394179B1 (fr)	2006-07-26
CA2220515A1 (fr)	1996-11-14
DE59611371D1 (de)	2006-09-07
EP0830376A1 (fr)	1998-03-25
ES2268232T3 (es)	2007-03-16
US6399333B1 (en)	2002-06-04

Legal Events

Date	Code	Title
2005-05-17	FF	Patent granted
2005-07-25	KB	Patent renewed
2006-08-01	KB	Patent renewed
2010-10-31	KB	Patent renewed
2014-05-28	KB	Patent renewed
2016-11-30	EXP	Patent expired

Publication	Publication Date	Title
US6399333B1 (en)	2002-06-04	Process for producing erythropoietin containing no animal proteins
Sassenfeld et al.	1984	A polypeptide fusion designed for the purification of recombinant proteins
US4667016A (en)	1987-05-19	Erythropoietin purification
Hansson et al.	1994	Single–Step Recovery of a Secreted Recombinant Protein by Expanded Bed Adsorption
US5310663A (en)	1994-05-10	Affinity peptides
US5643758A (en)	1997-07-01	Production and purification of a protein fused to a binding protein
US20200172589A1 (en)	2020-06-04	Purification of erythropoietin
Zechel	1980	Isolation of polymerization‐competent cytoplasmic actin by affinity chromatography on immobilized DNAse I using formamide as eluant
AU606578B2 (en)	1991-02-14	Chromatographic recovery of erythropoietin
CA1269799A (fr)	1990-05-29	Methode d'extraction des proteines au moyen d'un acide organique
Packman et al.	1982	An amino acid sequence in the active site of lipoamide dehydrogenase from Bacillus stearothermophilus
Lu et al.	1996	Isolation and Characterization of Human Tissue Kallikrein Produced inEscherichia coli: Biochemical Comparison to the Enzymatically Inactive Prokallikrein and Methionyl Kallikrein
Slobin	1979	Eucaryotic elongation factors Ts is an integral component of rabbit reticulocyte elongation factor 1
EP1015568B1 (fr)	2003-02-26	PROCEDE DE PRODUCTION DE rDSPA Alpha1
US5760187A (en)	1998-06-02	Purification process of a human growth hormone
KR960013572B1 (ko)	1996-10-09	인간 성장 호르몬의 정제방법
Jacobson et al.	1990	Rapid isolation of triosephosphate isomerase utilizing high-performance liquid chromatography
Kumar et al.	1988	Rapid isolation of lysyl-tRNA synthetase from rat liver
Mohan et al.	1990	Comparision of the methods available for the purification of hybrid β-galactosidase proteins produced under the control of an anaerobically-induced promoter
Mohanr et al.	1990	COMPARISION OF THE METHODS AVAILABLE FOR THE PURIFICATION OF HYBRID/3-GALACTOSIDASE PROTEINS PRODUCED UNDER THE CONTROL OF AN ANAEROBICALLY-INDUCED PROMOTER
KR20080082537A (ko)	2008-09-11	재조합 에리트로포이에틴의 신규한 정제방법