NO303451B1 - FremgangsmÕte for separasjon av en rÕproteinblanding - Google Patents
FremgangsmÕte for separasjon av en rÕproteinblanding Download PDFInfo
- Publication number
- NO303451B1 NO303451B1 NO901769A NO901769A NO303451B1 NO 303451 B1 NO303451 B1 NO 303451B1 NO 901769 A NO901769 A NO 901769A NO 901769 A NO901769 A NO 901769A NO 303451 B1 NO303451 B1 NO 303451B1
- Authority
- NO
- Norway
- Prior art keywords
- protein
- exchange resin
- ion exchange
- csf
- proteins
- Prior art date
Links
- 238000000034 method Methods 0.000 title claims abstract description 40
- 235000019750 Crude protein Nutrition 0.000 title claims abstract description 21
- 239000000203 mixture Substances 0.000 title claims description 16
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 90
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 90
- 102000004457 Granulocyte-Macrophage Colony-Stimulating Factor Human genes 0.000 claims abstract description 38
- 108010017213 Granulocyte-Macrophage Colony-Stimulating Factor Proteins 0.000 claims abstract description 38
- NWUYHJFMYQTDRP-UHFFFAOYSA-N 1,2-bis(ethenyl)benzene;1-ethenyl-2-ethylbenzene;styrene Chemical compound C=CC1=CC=CC=C1.CCC1=CC=CC=C1C=C.C=CC1=CC=CC=C1C=C NWUYHJFMYQTDRP-UHFFFAOYSA-N 0.000 claims abstract description 23
- 239000012535 impurity Substances 0.000 claims abstract description 22
- 239000003456 ion exchange resin Substances 0.000 claims description 24
- 229920003303 ion-exchange polymer Polymers 0.000 claims description 24
- 238000000926 separation method Methods 0.000 claims description 16
- 239000000499 gel Substances 0.000 claims description 8
- 238000005094 computer simulation Methods 0.000 claims description 7
- 238000002523 gelfiltration Methods 0.000 claims description 5
- 102000006992 Interferon-alpha Human genes 0.000 claims description 4
- 108010047761 Interferon-alpha Proteins 0.000 claims description 4
- 238000004440 column chromatography Methods 0.000 claims description 4
- 102000004411 Antithrombin III Human genes 0.000 claims description 3
- 108090000935 Antithrombin III Proteins 0.000 claims description 3
- 102100021809 Chorionic somatomammotropin hormone 1 Human genes 0.000 claims description 3
- 102000003951 Erythropoietin Human genes 0.000 claims description 3
- 108090000394 Erythropoietin Proteins 0.000 claims description 3
- 108010051696 Growth Hormone Proteins 0.000 claims description 3
- 101000895818 Homo sapiens Chorionic somatomammotropin hormone 1 Proteins 0.000 claims description 3
- 101000956228 Homo sapiens Chorionic somatomammotropin hormone 2 Proteins 0.000 claims description 3
- 102000013566 Plasminogen Human genes 0.000 claims description 3
- 108010051456 Plasminogen Proteins 0.000 claims description 3
- 108010057464 Prolactin Proteins 0.000 claims description 3
- 102100024819 Prolactin Human genes 0.000 claims description 3
- 102100038803 Somatotropin Human genes 0.000 claims description 3
- 102000019197 Superoxide Dismutase Human genes 0.000 claims description 3
- 108010012715 Superoxide dismutase Proteins 0.000 claims description 3
- 102000003990 Urokinase-type plasminogen activator Human genes 0.000 claims description 3
- 108090000435 Urokinase-type plasminogen activator Proteins 0.000 claims description 3
- 229960005348 antithrombin iii Drugs 0.000 claims description 3
- 229940105423 erythropoietin Drugs 0.000 claims description 3
- 239000000122 growth hormone Substances 0.000 claims description 3
- 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 description 3
- 229940097325 prolactin Drugs 0.000 claims description 3
- 229960005356 urokinase Drugs 0.000 claims description 3
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 claims description 2
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 claims description 2
- 102000011409 Transcobalamins Human genes 0.000 claims description 2
- 108010023603 Transcobalamins Proteins 0.000 claims description 2
- 239000003957 anion exchange resin Substances 0.000 claims 1
- 238000004255 ion exchange chromatography Methods 0.000 abstract description 8
- 239000003729 cation exchange resin Substances 0.000 abstract description 2
- 238000000746 purification Methods 0.000 abstract description 2
- 235000018102 proteins Nutrition 0.000 description 71
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 24
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 20
- 238000004587 chromatography analysis Methods 0.000 description 16
- 239000000872 buffer Substances 0.000 description 13
- 239000011780 sodium chloride Substances 0.000 description 10
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 9
- 238000001155 isoelectric focusing Methods 0.000 description 9
- 210000004027 cell Anatomy 0.000 description 8
- 239000000243 solution Substances 0.000 description 8
- 239000002299 complementary DNA Substances 0.000 description 7
- 238000011068 loading method Methods 0.000 description 7
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 7
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 6
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 6
- 235000011130 ammonium sulphate Nutrition 0.000 description 6
- OWMVSZAMULFTJU-UHFFFAOYSA-N bis-tris Chemical compound OCCN(CCO)C(CO)(CO)CO OWMVSZAMULFTJU-UHFFFAOYSA-N 0.000 description 6
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 description 6
- 229920000936 Agarose Polymers 0.000 description 5
- 229920002307 Dextran Polymers 0.000 description 5
- NIXOWILDQLNWCW-UHFFFAOYSA-N acrylic acid group Chemical group C(C=C)(=O)O NIXOWILDQLNWCW-UHFFFAOYSA-N 0.000 description 5
- 150000001412 amines Chemical group 0.000 description 5
- 229920002678 cellulose Polymers 0.000 description 5
- 239000001913 cellulose Substances 0.000 description 5
- 238000010828 elution Methods 0.000 description 5
- 239000000463 material Substances 0.000 description 5
- 229920002684 Sepharose Polymers 0.000 description 4
- 235000001014 amino acid Nutrition 0.000 description 4
- 229940024606 amino acid Drugs 0.000 description 4
- 150000001413 amino acids Chemical class 0.000 description 4
- 238000001502 gel electrophoresis Methods 0.000 description 4
- 238000001641 gel filtration chromatography Methods 0.000 description 4
- 238000005342 ion exchange Methods 0.000 description 4
- 239000002244 precipitate Substances 0.000 description 4
- 238000005119 centrifugation Methods 0.000 description 3
- 239000008367 deionised water Substances 0.000 description 3
- 229910021641 deionized water Inorganic materials 0.000 description 3
- 108020004999 messenger RNA Proteins 0.000 description 3
- 238000001556 precipitation Methods 0.000 description 3
- 108090000765 processed proteins & peptides Proteins 0.000 description 3
- 230000004850 protein–protein interaction Effects 0.000 description 3
- 230000002797 proteolythic effect Effects 0.000 description 3
- 150000003839 salts Chemical class 0.000 description 3
- 125000001273 sulfonato group Chemical group [O-]S(*)(=O)=O 0.000 description 3
- 239000006228 supernatant Substances 0.000 description 3
- 125000000022 2-aminoethyl group Chemical group [H]C([*])([H])C([H])([H])N([H])[H] 0.000 description 2
- 241000588724 Escherichia coli Species 0.000 description 2
- 101710190786 PI protein Proteins 0.000 description 2
- 239000012614 Q-Sepharose Substances 0.000 description 2
- 239000012506 Sephacryl® Substances 0.000 description 2
- 238000004458 analytical method Methods 0.000 description 2
- 238000011210 chromatographic step Methods 0.000 description 2
- 230000000295 complement effect Effects 0.000 description 2
- 239000000287 crude extract Substances 0.000 description 2
- 238000011161 development Methods 0.000 description 2
- 230000018109 developmental process Effects 0.000 description 2
- 238000009826 distribution Methods 0.000 description 2
- 238000001962 electrophoresis Methods 0.000 description 2
- 230000001747 exhibiting effect Effects 0.000 description 2
- 238000001914 filtration Methods 0.000 description 2
- 238000005194 fractionation Methods 0.000 description 2
- VNWKTOKETHGBQD-UHFFFAOYSA-N methane Chemical compound C VNWKTOKETHGBQD-UHFFFAOYSA-N 0.000 description 2
- 229920001184 polypeptide Polymers 0.000 description 2
- 102000004196 processed proteins & peptides Human genes 0.000 description 2
- 239000000047 product Substances 0.000 description 2
- 239000011347 resin Substances 0.000 description 2
- 229920005989 resin Polymers 0.000 description 2
- 238000012552 review Methods 0.000 description 2
- 239000001488 sodium phosphate Substances 0.000 description 2
- 229910000162 sodium phosphate Inorganic materials 0.000 description 2
- BDHFUVZGWQCTTF-UHFFFAOYSA-M sulfonate Chemical compound [O-]S(=O)=O BDHFUVZGWQCTTF-UHFFFAOYSA-M 0.000 description 2
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 2
- 239000008215 water for injection Substances 0.000 description 2
- GHCZTIFQWKKGSB-UHFFFAOYSA-N 2-hydroxypropane-1,2,3-tricarboxylic acid;phosphoric acid Chemical compound OP(O)(O)=O.OC(=O)CC(O)(C(O)=O)CC(O)=O GHCZTIFQWKKGSB-UHFFFAOYSA-N 0.000 description 1
- QFVHZQCOUORWEI-UHFFFAOYSA-N 4-[(4-anilino-5-sulfonaphthalen-1-yl)diazenyl]-5-hydroxynaphthalene-2,7-disulfonic acid Chemical compound C=12C(O)=CC(S(O)(=O)=O)=CC2=CC(S(O)(=O)=O)=CC=1N=NC(C1=CC=CC(=C11)S(O)(=O)=O)=CC=C1NC1=CC=CC=C1 QFVHZQCOUORWEI-UHFFFAOYSA-N 0.000 description 1
- VYZAMTAEIAYCRO-UHFFFAOYSA-N Chromium Chemical compound [Cr] VYZAMTAEIAYCRO-UHFFFAOYSA-N 0.000 description 1
- KRKNYBCHXYNGOX-UHFFFAOYSA-K Citrate Chemical compound [O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O KRKNYBCHXYNGOX-UHFFFAOYSA-K 0.000 description 1
- 108020004635 Complementary DNA Proteins 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 101000746373 Homo sapiens Granulocyte-macrophage colony-stimulating factor Proteins 0.000 description 1
- 102000014150 Interferons Human genes 0.000 description 1
- 108010050904 Interferons Proteins 0.000 description 1
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 1
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 1
- 125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 description 1
- 229910019142 PO4 Inorganic materials 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
- 239000004473 Threonine Substances 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 235000004279 alanine Nutrition 0.000 description 1
- 125000003295 alanine group Chemical group N[C@@H](C)C(=O)* 0.000 description 1
- 238000012870 ammonium sulfate precipitation Methods 0.000 description 1
- 239000001166 ammonium sulphate Substances 0.000 description 1
- 230000003321 amplification Effects 0.000 description 1
- 238000005349 anion exchange Methods 0.000 description 1
- 238000005571 anion exchange chromatography Methods 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- JXLHNMVSKXFWAO-UHFFFAOYSA-N azane;7-fluoro-2,1,3-benzoxadiazole-4-sulfonic acid Chemical compound N.OS(=O)(=O)C1=CC=C(F)C2=NON=C12 JXLHNMVSKXFWAO-UHFFFAOYSA-N 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 239000013602 bacteriophage vector Substances 0.000 description 1
- 230000004071 biological effect Effects 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
- 239000007853 buffer solution Substances 0.000 description 1
- 238000010804 cDNA synthesis Methods 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 238000005277 cation exchange chromatography Methods 0.000 description 1
- 150000001768 cations Chemical class 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 238000013375 chromatographic separation Methods 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 239000012228 culture supernatant Substances 0.000 description 1
- 238000013499 data model Methods 0.000 description 1
- 239000007857 degradation product Substances 0.000 description 1
- 230000000368 destabilizing effect Effects 0.000 description 1
- 238000007865 diluting Methods 0.000 description 1
- 238000010494 dissociation reaction Methods 0.000 description 1
- 230000005593 dissociations Effects 0.000 description 1
- 230000000694 effects Effects 0.000 description 1
- 230000009881 electrostatic interaction Effects 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 239000006167 equilibration buffer Substances 0.000 description 1
- 239000013604 expression vector Substances 0.000 description 1
- 239000000284 extract Substances 0.000 description 1
- 239000000706 filtrate Substances 0.000 description 1
- 239000012467 final product Substances 0.000 description 1
- 210000003714 granulocyte Anatomy 0.000 description 1
- 229920001519 homopolymer Polymers 0.000 description 1
- 102000046157 human CSF2 Human genes 0.000 description 1
- 238000004191 hydrophobic interaction chromatography Methods 0.000 description 1
- 125000004029 hydroxymethyl group Chemical group [H]OC([H])([H])* 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 229940047124 interferons Drugs 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- 229960000310 isoleucine Drugs 0.000 description 1
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 1
- 238000005304 joining Methods 0.000 description 1
- 210000000265 leukocyte Anatomy 0.000 description 1
- 210000002540 macrophage Anatomy 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
- 210000004962 mammalian cell Anatomy 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 229910052751 metal Inorganic materials 0.000 description 1
- 239000002184 metal Substances 0.000 description 1
- 238000003199 nucleic acid amplification method Methods 0.000 description 1
- 239000002773 nucleotide Substances 0.000 description 1
- 125000003729 nucleotide group Chemical group 0.000 description 1
- 239000008188 pellet Substances 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 239000013600 plasmid vector Substances 0.000 description 1
- 238000007747 plating Methods 0.000 description 1
- 230000010287 polarization Effects 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 239000011148 porous material Substances 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 230000037452 priming Effects 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 230000017854 proteolysis Effects 0.000 description 1
- 238000011268 retreatment Methods 0.000 description 1
- 238000001223 reverse osmosis Methods 0.000 description 1
- 238000004366 reverse phase liquid chromatography Methods 0.000 description 1
- 238000010839 reverse transcription Methods 0.000 description 1
- 238000004007 reversed phase HPLC Methods 0.000 description 1
- 108010053455 riboflavin-binding protein Proteins 0.000 description 1
- 239000012266 salt solution Substances 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 230000000087 stabilizing effect Effects 0.000 description 1
- 238000010186 staining Methods 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 230000009466 transformation Effects 0.000 description 1
- 238000000108 ultra-filtration Methods 0.000 description 1
- 210000005253 yeast cell Anatomy 0.000 description 1
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
- C07K14/52—Cytokines; Lymphokines; Interferons
- C07K14/53—Colony-stimulating factor [CSF]
- C07K14/535—Granulocyte CSF; Granulocyte-macrophage CSF
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01J—CHEMICAL OR PHYSICAL PROCESSES, e.g. CATALYSIS OR COLLOID CHEMISTRY; THEIR RELEVANT APPARATUS
- B01J39/00—Cation exchange; Use of material as cation exchangers; Treatment of material for improving the cation exchange properties
- B01J39/26—Cation exchangers for chromatographic processes
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/14—Extraction; Separation; Purification
- C07K1/16—Extraction; Separation; Purification by chromatography
- C07K1/18—Ion-exchange chromatography
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Analytical Chemistry (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Immunology (AREA)
- Toxicology (AREA)
- Zoology (AREA)
- Gastroenterology & Hepatology (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Treatment Of Liquids With Adsorbents In General (AREA)
- Ultra Sonic Daignosis Equipment (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Enzymes And Modification Thereof (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US11188687A | 1987-10-23 | 1987-10-23 | |
| PCT/US1988/003589 WO1989003840A1 (en) | 1987-10-23 | 1988-10-19 | Method of purifying protein |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| NO901769L NO901769L (no) | 1990-04-20 |
| NO901769D0 NO901769D0 (no) | 1990-04-20 |
| NO303451B1 true NO303451B1 (no) | 1998-07-13 |
Family
ID=22340970
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| NO901769A NO303451B1 (no) | 1987-10-23 | 1990-04-20 | FremgangsmÕte for separasjon av en rÕproteinblanding |
Country Status (21)
| Country | Link |
|---|---|
| EP (2) | EP0313343B2 (es) |
| JP (1) | JPH0788395B2 (es) |
| KR (1) | KR930008447B1 (es) |
| CN (1) | CN1031943C (es) |
| AT (1) | ATE121418T1 (es) |
| AU (1) | AU626008B2 (es) |
| DE (1) | DE3853610T3 (es) |
| DK (1) | DK99690D0 (es) |
| ES (1) | ES2070855T5 (es) |
| FI (1) | FI103974B1 (es) |
| HU (1) | HU204537B (es) |
| IE (1) | IE72219B1 (es) |
| IL (1) | IL88118A (es) |
| MY (1) | MY108512A (es) |
| NO (1) | NO303451B1 (es) |
| NZ (1) | NZ226651A (es) |
| OA (1) | OA09787A (es) |
| PT (1) | PT88813B (es) |
| TN (1) | TNSN88111A1 (es) |
| WO (1) | WO1989003840A1 (es) |
| ZA (1) | ZA887862B (es) |
Families Citing this family (18)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE68929566D1 (de) * | 1988-05-13 | 2010-01-28 | Amgen Inc | Verfahren zur Isolierung und Reinigung von G-CSF |
| US7217689B1 (en) | 1989-10-13 | 2007-05-15 | Amgen Inc. | Glycosylation analogs of erythropoietin |
| US5110913A (en) * | 1990-05-25 | 1992-05-05 | Miles Inc. | Antibody purification method |
| US5463029A (en) * | 1992-11-23 | 1995-10-31 | Immunex Corporation | Purification of fusion proteins comprising GM-CSF and IL-3 |
| JPH09502728A (ja) * | 1993-09-15 | 1997-03-18 | アルファ セラピューティク コーポレイション | α▲下１▼−酸性糖タンパク質の精製方法及び精製物 |
| US5808011A (en) * | 1996-07-01 | 1998-09-15 | Biopure Corporation | Method for chromatographic removal of prions |
| US7304150B1 (en) | 1998-10-23 | 2007-12-04 | Amgen Inc. | Methods and compositions for the prevention and treatment of anemia |
| ES2208305T3 (es) | 1999-04-08 | 2004-06-16 | Genentech, Inc. | Composicion basada en polipeptidos de carga opuesta.. |
| ES2626268T3 (es) * | 2002-09-11 | 2017-07-24 | Chugai Seiyaku Kabushiki Kaisha | Método de purificación de proteínas |
| DE10360841A1 (de) * | 2003-12-20 | 2005-07-14 | Henkel Kgaa | Helle, stabile, staub- und geruchsarme Enzymgranulate |
| KR101660575B1 (ko) * | 2005-03-11 | 2016-09-27 | 와이어쓰 엘엘씨 | 약한 분배성 크로마토그래피법 |
| SE529259C2 (sv) * | 2005-08-31 | 2007-06-12 | Ge Healthcare Bio Sciences Ab | Tillverkning av kromarografimatriser, en kromarografimatris, en vätskekromatografikolonn, prcess för att isolera målföreningar och användning av en kromarografimatris för vätskekromatografi |
| AU2007317200B8 (en) * | 2006-11-10 | 2012-02-02 | Agriculture Victoria Services Pty Ltd. | Process for the preparation of angiogenin |
| CN101556261B (zh) * | 2009-05-25 | 2012-01-11 | 北京理工大学 | 微管内等电聚焦和剪断吹出培养测定微生物等电点的方法 |
| CN101556260B (zh) * | 2009-05-25 | 2012-01-11 | 北京理工大学 | 固定化pH梯度毛细管等电聚焦测定微生物等电点的方法 |
| WO2013075740A1 (en) * | 2011-11-23 | 2013-05-30 | Sanofi | Antibody purification method |
| TR201815709T4 (tr) * | 2011-12-22 | 2018-11-21 | Hoffmann La Roche | İyon değişim membranı kromatografisi. |
| EP2994485B1 (en) | 2013-05-06 | 2018-01-10 | Sanofi | Continuous multistep process for purifying antibodies |
Family Cites Families (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4658018A (en) * | 1984-03-13 | 1987-04-14 | Immunex Corporation | Process for producing homogeneous colony stimulating factor |
| IL76360A0 (en) * | 1984-09-26 | 1986-01-31 | Takeda Chemical Industries Ltd | Mutual separation of proteins |
| ZA872781B (en) * | 1986-05-19 | 1987-10-05 | Immunology Ventures | B-cell stimulating factor |
-
1988
- 1988-10-19 AT AT88309824T patent/ATE121418T1/de not_active IP Right Cessation
- 1988-10-19 HU HU886264A patent/HU204537B/hu not_active IP Right Cessation
- 1988-10-19 JP JP63508950A patent/JPH0788395B2/ja not_active Expired - Lifetime
- 1988-10-19 EP EP88309824A patent/EP0313343B2/en not_active Expired - Lifetime
- 1988-10-19 DE DE3853610T patent/DE3853610T3/de not_active Expired - Fee Related
- 1988-10-19 KR KR1019890701131A patent/KR930008447B1/ko not_active IP Right Cessation
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- 1988-10-19 WO PCT/US1988/003589 patent/WO1989003840A1/en active IP Right Grant
- 1988-10-19 EP EP88909648A patent/EP0391934A1/en active Pending
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1990
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