NO310855B1 - Fremgangsmåte for rensing av protein - Google Patents
Fremgangsmåte for rensing av protein Download PDFInfo
- Publication number
- NO310855B1 NO310855B1 NO19943546A NO943546A NO310855B1 NO 310855 B1 NO310855 B1 NO 310855B1 NO 19943546 A NO19943546 A NO 19943546A NO 943546 A NO943546 A NO 943546A NO 310855 B1 NO310855 B1 NO 310855B1
- Authority
- NO
- Norway
- Prior art keywords
- protein
- substituted
- chromatography
- support
- ethylene glycol
- Prior art date
Links
- 108090000623 proteins and genes Proteins 0.000 title claims description 113
- 102000004169 proteins and genes Human genes 0.000 title claims description 103
- 238000000034 method Methods 0.000 title claims description 42
- 108010047295 complement receptors Proteins 0.000 claims abstract description 42
- 102000006834 complement receptors Human genes 0.000 claims abstract description 42
- 238000000746 purification Methods 0.000 claims abstract description 24
- 238000004191 hydrophobic interaction chromatography Methods 0.000 claims description 46
- 239000012634 fragment Substances 0.000 claims description 25
- 230000003993 interaction Effects 0.000 claims description 25
- 239000002609 medium Substances 0.000 claims description 20
- 238000001542 size-exclusion chromatography Methods 0.000 claims description 19
- 229920001577 copolymer Polymers 0.000 claims description 17
- 230000000295 complement effect Effects 0.000 claims description 15
- 230000002209 hydrophobic effect Effects 0.000 claims description 15
- 229920000936 Agarose Polymers 0.000 claims description 14
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 claims description 14
- 229910052921 ammonium sulfate Inorganic materials 0.000 claims description 14
- 235000011130 ammonium sulphate Nutrition 0.000 claims description 14
- 230000001143 conditioned effect Effects 0.000 claims description 13
- 239000000203 mixture Substances 0.000 claims description 12
- 150000003839 salts Chemical class 0.000 claims description 12
- 238000005341 cation exchange Methods 0.000 claims description 11
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 claims description 10
- 239000006143 cell culture medium Substances 0.000 claims description 10
- 239000000872 buffer Substances 0.000 claims description 9
- 238000005277 cation exchange chromatography Methods 0.000 claims description 9
- 238000010828 elution Methods 0.000 claims description 9
- 238000004255 ion exchange chromatography Methods 0.000 claims description 8
- MZVQCMJNVPIDEA-UHFFFAOYSA-N [CH2]CN(CC)CC Chemical group [CH2]CN(CC)CC MZVQCMJNVPIDEA-UHFFFAOYSA-N 0.000 claims description 7
- 125000002057 carboxymethyl group Chemical group [H]OC(=O)C([H])([H])[*] 0.000 claims description 7
- 229920002307 Dextran Polymers 0.000 claims description 6
- 241000700605 Viruses Species 0.000 claims description 6
- 125000000217 alkyl group Chemical group 0.000 claims description 6
- 238000005571 anion exchange chromatography Methods 0.000 claims description 6
- 125000003118 aryl group Chemical group 0.000 claims description 6
- 230000002779 inactivation Effects 0.000 claims description 6
- -1 alkyl silica Chemical compound 0.000 claims description 5
- 238000012870 ammonium sulfate precipitation Methods 0.000 claims description 5
- 239000001963 growth medium Substances 0.000 claims description 5
- 150000001768 cations Chemical class 0.000 claims description 4
- 238000011084 recovery Methods 0.000 claims description 4
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N silicon dioxide Inorganic materials O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 claims description 4
- 239000011780 sodium chloride Substances 0.000 claims description 4
- 238000000108 ultra-filtration Methods 0.000 claims description 4
- 230000003612 virological effect Effects 0.000 claims description 4
- 238000005406 washing Methods 0.000 claims description 4
- 239000011324 bead Substances 0.000 claims description 3
- 238000011210 chromatographic step Methods 0.000 claims description 3
- 238000004108 freeze drying Methods 0.000 claims description 3
- 229920000620 organic polymer Polymers 0.000 claims description 3
- 229920002401 polyacrylamide Polymers 0.000 claims description 3
- 239000002952 polymeric resin Substances 0.000 claims description 3
- 230000008569 process Effects 0.000 claims description 3
- 239000000377 silicon dioxide Substances 0.000 claims description 3
- 102100030886 Complement receptor type 1 Human genes 0.000 claims description 2
- 230000001376 precipitating effect Effects 0.000 claims description 2
- 239000001488 sodium phosphate Substances 0.000 claims 4
- 229910000162 sodium phosphate Inorganic materials 0.000 claims 4
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 claims 4
- 238000005349 anion exchange Methods 0.000 claims 3
- 239000001913 cellulose Substances 0.000 claims 3
- 229920002678 cellulose Polymers 0.000 claims 3
- 239000007975 buffered saline Substances 0.000 claims 2
- 230000000415 inactivating effect Effects 0.000 claims 2
- VGGSQFUCUMXWEO-UHFFFAOYSA-N Ethene Chemical compound C=C VGGSQFUCUMXWEO-UHFFFAOYSA-N 0.000 claims 1
- 239000005977 Ethylene Substances 0.000 claims 1
- 230000007717 exclusion Effects 0.000 claims 1
- 229960000789 guanidine hydrochloride Drugs 0.000 claims 1
- PJJJBBJSCAKJQF-UHFFFAOYSA-N guanidinium chloride Chemical compound [Cl-].NC(N)=[NH2+] PJJJBBJSCAKJQF-UHFFFAOYSA-N 0.000 claims 1
- 239000012266 salt solution Substances 0.000 claims 1
- 239000012064 sodium phosphate buffer Substances 0.000 claims 1
- 238000004587 chromatography analysis Methods 0.000 abstract description 12
- 235000018102 proteins Nutrition 0.000 description 82
- 210000004027 cell Anatomy 0.000 description 41
- 239000000047 product Substances 0.000 description 25
- 239000000499 gel Substances 0.000 description 24
- 239000003446 ligand Substances 0.000 description 17
- 108020004414 DNA Proteins 0.000 description 11
- 229920005654 Sephadex Polymers 0.000 description 10
- 239000012507 Sephadex™ Substances 0.000 description 10
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 9
- 229920002684 Sepharose Polymers 0.000 description 9
- 102000005962 receptors Human genes 0.000 description 9
- 108020003175 receptors Proteins 0.000 description 9
- 102100022133 Complement C3 Human genes 0.000 description 8
- 101000901154 Homo sapiens Complement C3 Proteins 0.000 description 8
- 230000027455 binding Effects 0.000 description 8
- 239000000356 contaminant Substances 0.000 description 8
- 238000004519 manufacturing process Methods 0.000 description 8
- 239000011159 matrix material Substances 0.000 description 8
- 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 7
- 239000000463 material Substances 0.000 description 7
- 230000010412 perfusion Effects 0.000 description 7
- 101100351256 Caenorhabditis elegans ccm-3 gene Proteins 0.000 description 6
- 108020004635 Complementary DNA Proteins 0.000 description 6
- LYCAIKOWRPUZTN-UHFFFAOYSA-N Ethylene glycol Chemical compound OCCO LYCAIKOWRPUZTN-UHFFFAOYSA-N 0.000 description 6
- 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 6
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 6
- 238000010804 cDNA synthesis Methods 0.000 description 6
- 239000002299 complementary DNA Substances 0.000 description 6
- 239000012141 concentrate Substances 0.000 description 6
- 239000012091 fetal bovine serum Substances 0.000 description 6
- 230000006870 function Effects 0.000 description 6
- 239000008103 glucose Substances 0.000 description 6
- 108020004999 messenger RNA Proteins 0.000 description 6
- 238000001556 precipitation Methods 0.000 description 6
- 238000001742 protein purification Methods 0.000 description 6
- 230000000694 effects Effects 0.000 description 5
- 238000011068 loading method Methods 0.000 description 5
- 239000004005 microsphere Substances 0.000 description 5
- 239000000523 sample Substances 0.000 description 5
- 238000000926 separation method Methods 0.000 description 5
- 239000000243 solution Substances 0.000 description 5
- 238000003756 stirring Methods 0.000 description 5
- 238000011282 treatment Methods 0.000 description 5
- RYHBNJHYFVUHQT-UHFFFAOYSA-N 1,4-Dioxane Chemical compound C1COCCO1 RYHBNJHYFVUHQT-UHFFFAOYSA-N 0.000 description 4
- RNHDAKUGFHSZEV-UHFFFAOYSA-N 1,4-dioxane;hydrate Chemical compound O.C1COCCO1 RNHDAKUGFHSZEV-UHFFFAOYSA-N 0.000 description 4
- 108091028043 Nucleic acid sequence Proteins 0.000 description 4
- 150000001413 amino acids Chemical group 0.000 description 4
- 239000000969 carrier Substances 0.000 description 4
- 238000004113 cell culture Methods 0.000 description 4
- 239000002245 particle Substances 0.000 description 4
- 239000002244 precipitate Substances 0.000 description 4
- 238000002360 preparation method Methods 0.000 description 4
- 230000000717 retained effect Effects 0.000 description 4
- 239000002904 solvent Substances 0.000 description 4
- 238000001890 transfection Methods 0.000 description 4
- 239000013598 vector Substances 0.000 description 4
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 4
- 108010023729 Complement 3d Receptors Proteins 0.000 description 3
- 102000011412 Complement 3d Receptors Human genes 0.000 description 3
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- 101000727061 Homo sapiens Complement receptor type 1 Proteins 0.000 description 3
- 108020004511 Recombinant DNA Proteins 0.000 description 3
- 238000002835 absorbance Methods 0.000 description 3
- 230000004913 activation Effects 0.000 description 3
- 125000000129 anionic group Chemical group 0.000 description 3
- 125000000484 butyl group Chemical group [H]C([*])([H])C([H])([H])C([H])([H])C([H])([H])[H] 0.000 description 3
- 125000004432 carbon atom Chemical group C* 0.000 description 3
- 230000003196 chaotropic effect Effects 0.000 description 3
- 238000006243 chemical reaction Methods 0.000 description 3
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 3
- 238000010367 cloning Methods 0.000 description 3
- GYZLOYUZLJXAJU-UHFFFAOYSA-N diglycidyl ether Chemical compound C1OC1COCC1CO1 GYZLOYUZLJXAJU-UHFFFAOYSA-N 0.000 description 3
- 239000000706 filtrate Substances 0.000 description 3
- 238000011081 inoculation Methods 0.000 description 3
- 238000005342 ion exchange Methods 0.000 description 3
- 229960000485 methotrexate Drugs 0.000 description 3
- 239000012466 permeate Substances 0.000 description 3
- 125000001997 phenyl group Chemical group [H]C1=C([H])C([H])=C(*)C([H])=C1[H] 0.000 description 3
- 239000011148 porous material Substances 0.000 description 3
- 239000006152 selective media Substances 0.000 description 3
- 201000000596 systemic lupus erythematosus Diseases 0.000 description 3
- 108700028369 Alleles Proteins 0.000 description 2
- 101100365087 Arabidopsis thaliana SCRA gene Proteins 0.000 description 2
- KZMGYPLQYOPHEL-UHFFFAOYSA-N Boron trifluoride etherate Chemical compound FB(F)F.CCOCC KZMGYPLQYOPHEL-UHFFFAOYSA-N 0.000 description 2
- 241000283690 Bos taurus Species 0.000 description 2
- 108091026890 Coding region Proteins 0.000 description 2
- 241000699802 Cricetulus griseus Species 0.000 description 2
- 108090000288 Glycoproteins Proteins 0.000 description 2
- 102000003886 Glycoproteins Human genes 0.000 description 2
- 206010018910 Haemolysis Diseases 0.000 description 2
- 108010052369 Integrin alphaXbeta2 Proteins 0.000 description 2
- KFZMGEQAYNKOFK-UHFFFAOYSA-N Isopropanol Chemical compound CC(C)O KFZMGEQAYNKOFK-UHFFFAOYSA-N 0.000 description 2
- 101150105073 SCR1 gene Proteins 0.000 description 2
- 101100134054 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) NTG1 gene Proteins 0.000 description 2
- 238000001042 affinity chromatography Methods 0.000 description 2
- 235000001014 amino acid Nutrition 0.000 description 2
- 238000004458 analytical method Methods 0.000 description 2
- 150000001450 anions Chemical class 0.000 description 2
- 230000002587 anti-hemolytic effect Effects 0.000 description 2
- 230000015572 biosynthetic process Effects 0.000 description 2
- 125000002091 cationic group Chemical group 0.000 description 2
- 230000010261 cell growth Effects 0.000 description 2
- 108010052926 complement C3d,g Proteins 0.000 description 2
- 239000003636 conditioned culture medium Substances 0.000 description 2
- 238000010276 construction Methods 0.000 description 2
- 230000008878 coupling Effects 0.000 description 2
- 238000010168 coupling process Methods 0.000 description 2
- 238000005859 coupling reaction Methods 0.000 description 2
- 210000003743 erythrocyte Anatomy 0.000 description 2
- 239000013604 expression vector Substances 0.000 description 2
- 239000012894 fetal calf serum Substances 0.000 description 2
- 238000001914 filtration Methods 0.000 description 2
- 125000000524 functional group Chemical group 0.000 description 2
- 108020001507 fusion proteins Proteins 0.000 description 2
- 102000037865 fusion proteins Human genes 0.000 description 2
- 230000012010 growth Effects 0.000 description 2
- 230000008588 hemolysis Effects 0.000 description 2
- 102000046508 human CR1 Human genes 0.000 description 2
- 239000003112 inhibitor Substances 0.000 description 2
- 150000002500 ions Chemical class 0.000 description 2
- 229920002521 macromolecule Polymers 0.000 description 2
- 230000001404 mediated effect Effects 0.000 description 2
- 239000012528 membrane Substances 0.000 description 2
- 238000001471 micro-filtration Methods 0.000 description 2
- 229920001542 oligosaccharide Polymers 0.000 description 2
- 150000002482 oligosaccharides Chemical class 0.000 description 2
- 230000035515 penetration Effects 0.000 description 2
- 239000013612 plasmid Substances 0.000 description 2
- 229920001184 polypeptide Polymers 0.000 description 2
- 102000004196 processed proteins & peptides Human genes 0.000 description 2
- 108090000765 processed proteins & peptides Proteins 0.000 description 2
- 230000017854 proteolysis Effects 0.000 description 2
- 230000002797 proteolythic effect Effects 0.000 description 2
- 239000012465 retentate Substances 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 125000001424 substituent group Chemical group 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- 239000004094 surface-active agent Substances 0.000 description 2
- 238000003786 synthesis reaction Methods 0.000 description 2
- 230000007704 transition Effects 0.000 description 2
- VYEWZWBILJHHCU-OMQUDAQFSA-N (e)-n-[(2s,3r,4r,5r,6r)-2-[(2r,3r,4s,5s,6s)-3-acetamido-5-amino-4-hydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-6-[2-[(2r,3s,4r,5r)-5-(2,4-dioxopyrimidin-1-yl)-3,4-dihydroxyoxolan-2-yl]-2-hydroxyethyl]-4,5-dihydroxyoxan-3-yl]-5-methylhex-2-enamide Chemical compound N1([C@@H]2O[C@@H]([C@H]([C@H]2O)O)C(O)C[C@@H]2[C@H](O)[C@H](O)[C@H]([C@@H](O2)O[C@@H]2[C@@H]([C@@H](O)[C@H](N)[C@@H](CO)O2)NC(C)=O)NC(=O)/C=C/CC(C)C)C=CC(=O)NC1=O VYEWZWBILJHHCU-OMQUDAQFSA-N 0.000 description 1
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 1
- 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 description 1
- 125000000022 2-aminoethyl group Chemical group [H]C([*])([H])C([H])([H])N([H])[H] 0.000 description 1
- GUPXYSSGJWIURR-UHFFFAOYSA-N 3-octoxypropane-1,2-diol Chemical compound CCCCCCCCOCC(O)CO GUPXYSSGJWIURR-UHFFFAOYSA-N 0.000 description 1
- XTWYTFMLZFPYCI-KQYNXXCUSA-N 5'-adenylphosphoric acid Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@@H]1O[C@H](COP(O)(=O)OP(O)(O)=O)[C@@H](O)[C@H]1O XTWYTFMLZFPYCI-KQYNXXCUSA-N 0.000 description 1
- 241000251468 Actinopterygii Species 0.000 description 1
- XTWYTFMLZFPYCI-UHFFFAOYSA-N Adenosine diphosphate Natural products C1=NC=2C(N)=NC=NC=2N1C1OC(COP(O)(=O)OP(O)(O)=O)C(O)C1O XTWYTFMLZFPYCI-UHFFFAOYSA-N 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- 208000000104 Arthus reaction Diseases 0.000 description 1
- 241000193830 Bacillus <bacterium> Species 0.000 description 1
- HNNIWKQLJSNAEQ-UHFFFAOYSA-N Benzydamine hydrochloride Chemical compound Cl.C12=CC=CC=C2C(OCCCN(C)C)=NN1CC1=CC=CC=C1 HNNIWKQLJSNAEQ-UHFFFAOYSA-N 0.000 description 1
- 102000015081 Blood Coagulation Factors Human genes 0.000 description 1
- 108010039209 Blood Coagulation Factors Proteins 0.000 description 1
- 108010017384 Blood Proteins Proteins 0.000 description 1
- 102000004506 Blood Proteins Human genes 0.000 description 1
- 239000012619 Butyl Sepharose® Substances 0.000 description 1
- 101710159767 C4b-binding protein alpha chain Proteins 0.000 description 1
- 102100037084 C4b-binding protein alpha chain Human genes 0.000 description 1
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 1
- 239000004215 Carbon black (E152) Substances 0.000 description 1
- 206010057248 Cell death Diseases 0.000 description 1
- UDMBCSSLTHHNCD-UHFFFAOYSA-N Coenzym Q(11) Natural products C1=NC=2C(N)=NC=NC=2N1C1OC(COP(O)(O)=O)C(O)C1O UDMBCSSLTHHNCD-UHFFFAOYSA-N 0.000 description 1
- 108010078015 Complement C3b Proteins 0.000 description 1
- 108010053085 Complement Factor H Proteins 0.000 description 1
- 102000016550 Complement Factor H Human genes 0.000 description 1
- 108010069112 Complement System Proteins Proteins 0.000 description 1
- 102000000989 Complement System Proteins Human genes 0.000 description 1
- 102000003712 Complement factor B Human genes 0.000 description 1
- 108090000056 Complement factor B Proteins 0.000 description 1
- 229940124073 Complement inhibitor Drugs 0.000 description 1
- 101150074155 DHFR gene Proteins 0.000 description 1
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 1
- 238000002965 ELISA Methods 0.000 description 1
- 241000588722 Escherichia Species 0.000 description 1
- 239000012541 Fractogel® Substances 0.000 description 1
- 230000005526 G1 to G0 transition Effects 0.000 description 1
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 1
- 102000014702 Haptoglobin Human genes 0.000 description 1
- 108050005077 Haptoglobin Proteins 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 102000002265 Human Growth Hormone Human genes 0.000 description 1
- 108010000521 Human Growth Hormone Proteins 0.000 description 1
- 239000000854 Human Growth Hormone Substances 0.000 description 1
- 102000000588 Interleukin-2 Human genes 0.000 description 1
- 108010002350 Interleukin-2 Proteins 0.000 description 1
- 102000010789 Interleukin-2 Receptors Human genes 0.000 description 1
- 108010038453 Interleukin-2 Receptors Proteins 0.000 description 1
- 229920001202 Inulin Polymers 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
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 1
- 102000004083 Lymphotoxin-alpha Human genes 0.000 description 1
- 108090000542 Lymphotoxin-alpha Proteins 0.000 description 1
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- 108010052285 Membrane Proteins Proteins 0.000 description 1
- 102000016943 Muramidase Human genes 0.000 description 1
- 108010014251 Muramidase Proteins 0.000 description 1
- 101100366942 Mus musculus Ston1 gene Proteins 0.000 description 1
- 208000009525 Myocarditis Diseases 0.000 description 1
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
- 229920002274 Nalgene Polymers 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 206010057249 Phagocytosis Diseases 0.000 description 1
- 241000276498 Pollachius virens Species 0.000 description 1
- 241000235070 Saccharomyces Species 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- 239000012506 Sephacryl® Substances 0.000 description 1
- 210000001744 T-lymphocyte Anatomy 0.000 description 1
- 108010022394 Threonine synthase Proteins 0.000 description 1
- 108060008682 Tumor Necrosis Factor Proteins 0.000 description 1
- 102000000852 Tumor Necrosis Factor-alpha Human genes 0.000 description 1
- YJQCOFNZVFGCAF-UHFFFAOYSA-N Tunicamycin II Natural products O1C(CC(O)C2C(C(O)C(O2)N2C(NC(=O)C=C2)=O)O)C(O)C(O)C(NC(=O)C=CCCCCCCCCC(C)C)C1OC1OC(CO)C(O)C(O)C1NC(C)=O YJQCOFNZVFGCAF-UHFFFAOYSA-N 0.000 description 1
- 206010053614 Type III immune complex mediated reaction Diseases 0.000 description 1
- 239000012190 activator Substances 0.000 description 1
- UDMBCSSLTHHNCD-KQYNXXCUSA-N adenosine 5'-monophosphate Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@@H]1O[C@H](COP(O)(O)=O)[C@@H](O)[C@H]1O UDMBCSSLTHHNCD-KQYNXXCUSA-N 0.000 description 1
- LNQVTSROQXJCDD-UHFFFAOYSA-N adenosine monophosphate Natural products C1=NC=2C(N)=NC=NC=2N1C1OC(CO)C(OP(O)(O)=O)C1O LNQVTSROQXJCDD-UHFFFAOYSA-N 0.000 description 1
- 239000003463 adsorbent Substances 0.000 description 1
- 230000002776 aggregation Effects 0.000 description 1
- 238000004220 aggregation Methods 0.000 description 1
- 125000003295 alanine group Chemical group N[C@@H](C)C(=O)* 0.000 description 1
- 150000003973 alkyl amines Chemical class 0.000 description 1
- 150000001412 amines Chemical group 0.000 description 1
- 125000000539 amino acid group Chemical group 0.000 description 1
- 230000003698 anagen phase Effects 0.000 description 1
- 210000004102 animal cell Anatomy 0.000 description 1
- 239000003957 anion exchange resin Substances 0.000 description 1
- 239000000427 antigen Substances 0.000 description 1
- 108091007433 antigens Proteins 0.000 description 1
- 102000036639 antigens Human genes 0.000 description 1
- 239000012736 aqueous medium Substances 0.000 description 1
- 239000003125 aqueous solvent Substances 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 235000003704 aspartic acid Nutrition 0.000 description 1
- 239000012298 atmosphere Substances 0.000 description 1
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 1
- 210000003719 b-lymphocyte Anatomy 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- MSWZFWKMSRAUBD-UHFFFAOYSA-N beta-D-galactosamine Natural products NC1C(O)OC(CO)C(O)C1O MSWZFWKMSRAUBD-UHFFFAOYSA-N 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
- 230000004071 biological effect Effects 0.000 description 1
- 239000003114 blood coagulation factor Substances 0.000 description 1
- 229940019700 blood coagulation factors Drugs 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 239000011575 calcium Substances 0.000 description 1
- 229910052791 calcium Inorganic materials 0.000 description 1
- 150000001720 carbohydrates Chemical class 0.000 description 1
- 235000014633 carbohydrates Nutrition 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 238000012832 cell culture technique Methods 0.000 description 1
- 210000002421 cell wall Anatomy 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 230000035605 chemotaxis Effects 0.000 description 1
- 238000005352 clarification Methods 0.000 description 1
- 238000000975 co-precipitation Methods 0.000 description 1
- 238000002648 combination therapy Methods 0.000 description 1
- 230000024203 complement activation Effects 0.000 description 1
- 239000004074 complement inhibitor Substances 0.000 description 1
- 230000004154 complement system Effects 0.000 description 1
- 239000012468 concentrated sample Substances 0.000 description 1
- 238000012136 culture method Methods 0.000 description 1
- ATDGTVJJHBUTRL-UHFFFAOYSA-N cyanogen bromide Chemical compound BrC#N ATDGTVJJHBUTRL-UHFFFAOYSA-N 0.000 description 1
- 230000009089 cytolysis Effects 0.000 description 1
- 210000005220 cytoplasmic tail Anatomy 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 230000002950 deficient Effects 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 238000012217 deletion Methods 0.000 description 1
- 230000037430 deletion Effects 0.000 description 1
- 229940061607 dibasic sodium phosphate Drugs 0.000 description 1
- 235000015872 dietary supplement Nutrition 0.000 description 1
- 102000004419 dihydrofolate reductase Human genes 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- BNIILDVGGAEEIG-UHFFFAOYSA-L disodium hydrogen phosphate Chemical compound [Na+].[Na+].OP([O-])([O-])=O BNIILDVGGAEEIG-UHFFFAOYSA-L 0.000 description 1
- 208000035475 disorder Diseases 0.000 description 1
- 238000004090 dissolution Methods 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- 239000012636 effector Substances 0.000 description 1
- 239000002158 endotoxin Substances 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 238000006911 enzymatic reaction Methods 0.000 description 1
- 239000013613 expression plasmid Substances 0.000 description 1
- 239000003527 fibrinolytic agent Substances 0.000 description 1
- 210000000285 follicular dendritic cell Anatomy 0.000 description 1
- 238000009472 formulation Methods 0.000 description 1
- BTCSSZJGUNDROE-UHFFFAOYSA-N gamma-aminobutyric acid Chemical compound NCCCC(O)=O BTCSSZJGUNDROE-UHFFFAOYSA-N 0.000 description 1
- 238000001641 gel filtration chromatography Methods 0.000 description 1
- 238000005227 gel permeation chromatography Methods 0.000 description 1
- 238000002523 gelfiltration Methods 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 210000001282 glomerular podocyte Anatomy 0.000 description 1
- 229960002442 glucosamine Drugs 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 210000003714 granulocyte Anatomy 0.000 description 1
- 230000009931 harmful effect Effects 0.000 description 1
- 239000012510 hollow fiber Substances 0.000 description 1
- 210000005260 human cell Anatomy 0.000 description 1
- 230000004727 humoral immunity Effects 0.000 description 1
- 229930195733 hydrocarbon Natural products 0.000 description 1
- 229910052739 hydrogen Inorganic materials 0.000 description 1
- 239000001257 hydrogen Substances 0.000 description 1
- 239000002596 immunotoxin Substances 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 230000000977 initiatory effect Effects 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- JYJIGFIDKWBXDU-MNNPPOADSA-N inulin Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)OC[C@]1(OC[C@]2(OC[C@]3(OC[C@]4(OC[C@]5(OC[C@]6(OC[C@]7(OC[C@]8(OC[C@]9(OC[C@]%10(OC[C@]%11(OC[C@]%12(OC[C@]%13(OC[C@]%14(OC[C@]%15(OC[C@]%16(OC[C@]%17(OC[C@]%18(OC[C@]%19(OC[C@]%20(OC[C@]%21(OC[C@]%22(OC[C@]%23(OC[C@]%24(OC[C@]%25(OC[C@]%26(OC[C@]%27(OC[C@]%28(OC[C@]%29(OC[C@]%30(OC[C@]%31(OC[C@]%32(OC[C@]%33(OC[C@]%34(OC[C@]%35(OC[C@]%36(O[C@@H]%37[C@@H]([C@@H](O)[C@H](O)[C@@H](CO)O%37)O)[C@H]([C@H](O)[C@@H](CO)O%36)O)[C@H]([C@H](O)[C@@H](CO)O%35)O)[C@H]([C@H](O)[C@@H](CO)O%34)O)[C@H]([C@H](O)[C@@H](CO)O%33)O)[C@H]([C@H](O)[C@@H](CO)O%32)O)[C@H]([C@H](O)[C@@H](CO)O%31)O)[C@H]([C@H](O)[C@@H](CO)O%30)O)[C@H]([C@H](O)[C@@H](CO)O%29)O)[C@H]([C@H](O)[C@@H](CO)O%28)O)[C@H]([C@H](O)[C@@H](CO)O%27)O)[C@H]([C@H](O)[C@@H](CO)O%26)O)[C@H]([C@H](O)[C@@H](CO)O%25)O)[C@H]([C@H](O)[C@@H](CO)O%24)O)[C@H]([C@H](O)[C@@H](CO)O%23)O)[C@H]([C@H](O)[C@@H](CO)O%22)O)[C@H]([C@H](O)[C@@H](CO)O%21)O)[C@H]([C@H](O)[C@@H](CO)O%20)O)[C@H]([C@H](O)[C@@H](CO)O%19)O)[C@H]([C@H](O)[C@@H](CO)O%18)O)[C@H]([C@H](O)[C@@H](CO)O%17)O)[C@H]([C@H](O)[C@@H](CO)O%16)O)[C@H]([C@H](O)[C@@H](CO)O%15)O)[C@H]([C@H](O)[C@@H](CO)O%14)O)[C@H]([C@H](O)[C@@H](CO)O%13)O)[C@H]([C@H](O)[C@@H](CO)O%12)O)[C@H]([C@H](O)[C@@H](CO)O%11)O)[C@H]([C@H](O)[C@@H](CO)O%10)O)[C@H]([C@H](O)[C@@H](CO)O9)O)[C@H]([C@H](O)[C@@H](CO)O8)O)[C@H]([C@H](O)[C@@H](CO)O7)O)[C@H]([C@H](O)[C@@H](CO)O6)O)[C@H]([C@H](O)[C@@H](CO)O5)O)[C@H]([C@H](O)[C@@H](CO)O4)O)[C@H]([C@H](O)[C@@H](CO)O3)O)[C@H]([C@H](O)[C@@H](CO)O2)O)[C@@H](O)[C@H](O)[C@@H](CO)O1 JYJIGFIDKWBXDU-MNNPPOADSA-N 0.000 description 1
- 229940029339 inulin Drugs 0.000 description 1
- 239000003456 ion exchange resin Substances 0.000 description 1
- 229920003303 ion-exchange polymer Polymers 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 229960000274 lysozyme Drugs 0.000 description 1
- 235000010335 lysozyme Nutrition 0.000 description 1
- 239000004325 lysozyme Substances 0.000 description 1
- 210000002540 macrophage Anatomy 0.000 description 1
- 238000012423 maintenance Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 108091005573 modified proteins Proteins 0.000 description 1
- 102000035118 modified proteins Human genes 0.000 description 1
- 239000003607 modifier Substances 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 210000001616 monocyte Anatomy 0.000 description 1
- 208000010125 myocardial infarction Diseases 0.000 description 1
- 230000017074 necrotic cell death Effects 0.000 description 1
- 210000000440 neutrophil Anatomy 0.000 description 1
- JOUIQRNQJGXQDC-ZYUZMQFOSA-L nicotinate D-ribonucleotide(2-) Chemical compound O1[C@H](COP([O-])([O-])=O)[C@@H](O)[C@@H](O)[C@@H]1[N+]1=CC=CC(C([O-])=O)=C1 JOUIQRNQJGXQDC-ZYUZMQFOSA-L 0.000 description 1
- 238000003199 nucleic acid amplification method Methods 0.000 description 1
- 108020004707 nucleic acids Proteins 0.000 description 1
- 102000039446 nucleic acids Human genes 0.000 description 1
- 150000007523 nucleic acids Chemical class 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- 125000002347 octyl group Chemical group [H]C([*])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])[H] 0.000 description 1
- 230000014207 opsonization Effects 0.000 description 1
- 239000003960 organic solvent Substances 0.000 description 1
- 210000001672 ovary Anatomy 0.000 description 1
- 229910052760 oxygen Inorganic materials 0.000 description 1
- 239000001301 oxygen Substances 0.000 description 1
- 238000010979 pH adjustment Methods 0.000 description 1
- 230000020477 pH reduction Effects 0.000 description 1
- 239000008188 pellet Substances 0.000 description 1
- 125000001147 pentyl group Chemical group C(CCCC)* 0.000 description 1
- 230000000737 periodic effect Effects 0.000 description 1
- 230000008782 phagocytosis Effects 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
- 239000008363 phosphate buffer Substances 0.000 description 1
- 230000004962 physiological condition Effects 0.000 description 1
- 229940012957 plasmin Drugs 0.000 description 1
- 230000008488 polyadenylation Effects 0.000 description 1
- 102000054765 polymorphisms of proteins Human genes 0.000 description 1
- 238000007781 pre-processing Methods 0.000 description 1
- 238000011045 prefiltration Methods 0.000 description 1
- 230000002265 prevention Effects 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 239000013587 production medium Substances 0.000 description 1
- 125000001436 propyl group Chemical group [H]C([*])([H])C([H])([H])C([H])([H])[H] 0.000 description 1
- 230000004952 protein activity Effects 0.000 description 1
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 1
- 239000002510 pyrogen Substances 0.000 description 1
- 239000002994 raw material Substances 0.000 description 1
- 239000011541 reaction mixture Substances 0.000 description 1
- 230000003134 recirculating effect Effects 0.000 description 1
- 238000010188 recombinant method Methods 0.000 description 1
- 230000019254 respiratory burst Effects 0.000 description 1
- 238000005185 salting out Methods 0.000 description 1
- 230000003248 secreting effect Effects 0.000 description 1
- 238000010187 selection method Methods 0.000 description 1
- 230000035939 shock Effects 0.000 description 1
- 238000007873 sieving Methods 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 238000001179 sorption measurement Methods 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 238000009987 spinning Methods 0.000 description 1
- 210000000952 spleen Anatomy 0.000 description 1
- 239000007858 starting material Substances 0.000 description 1
- 229960005202 streptokinase Drugs 0.000 description 1
- BDHFUVZGWQCTTF-UHFFFAOYSA-M sulfonate Chemical compound [O-]S(=O)=O BDHFUVZGWQCTTF-UHFFFAOYSA-M 0.000 description 1
- 239000013589 supplement Substances 0.000 description 1
- 229960000103 thrombolytic agent Drugs 0.000 description 1
- 238000013518 transcription Methods 0.000 description 1
- 230000035897 transcription Effects 0.000 description 1
- 230000001131 transforming effect Effects 0.000 description 1
- MEYZYGMYMLNUHJ-UHFFFAOYSA-N tunicamycin Natural products CC(C)CCCCCCCCCC=CC(=O)NC1C(O)C(O)C(CC(O)C2OC(C(O)C2O)N3C=CC(=O)NC3=O)OC1OC4OC(CO)C(O)C(O)C4NC(=O)C MEYZYGMYMLNUHJ-UHFFFAOYSA-N 0.000 description 1
- 241001430294 unidentified retrovirus Species 0.000 description 1
- 239000003981 vehicle Substances 0.000 description 1
- 239000011534 wash buffer Substances 0.000 description 1
- 230000003313 weakening effect Effects 0.000 description 1
Classifications
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01D—SEPARATION
- B01D15/00—Separating processes involving the treatment of liquids with solid sorbents; Apparatus therefor
- B01D15/08—Selective adsorption, e.g. chromatography
-
- 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
- C07K14/70596—Molecules with a "CD"-designation not provided for elsewhere
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01D—SEPARATION
- B01D15/00—Separating processes involving the treatment of liquids with solid sorbents; Apparatus therefor
- B01D15/08—Selective adsorption, e.g. chromatography
- B01D15/10—Selective adsorption, e.g. chromatography characterised by constructional or operational features
- B01D15/18—Selective adsorption, e.g. chromatography characterised by constructional or operational features relating to flow patterns
- B01D15/1864—Selective adsorption, e.g. chromatography characterised by constructional or operational features relating to flow patterns using two or more columns
- B01D15/1871—Selective adsorption, e.g. chromatography characterised by constructional or operational features relating to flow patterns using two or more columns placed in series
-
- 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
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01D—SEPARATION
- B01D15/00—Separating processes involving the treatment of liquids with solid sorbents; Apparatus therefor
- B01D15/08—Selective adsorption, e.g. chromatography
- B01D15/26—Selective adsorption, e.g. chromatography characterised by the separation mechanism
- B01D15/32—Bonded phase chromatography
- B01D15/325—Reversed phase
- B01D15/327—Reversed phase with hydrophobic interaction
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01D—SEPARATION
- B01D15/00—Separating processes involving the treatment of liquids with solid sorbents; Apparatus therefor
- B01D15/08—Selective adsorption, e.g. chromatography
- B01D15/26—Selective adsorption, e.g. chromatography characterised by the separation mechanism
- B01D15/34—Size selective separation, e.g. size exclusion chromatography, gel filtration, permeation
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01D—SEPARATION
- B01D15/00—Separating processes involving the treatment of liquids with solid sorbents; Apparatus therefor
- B01D15/08—Selective adsorption, e.g. chromatography
- B01D15/26—Selective adsorption, e.g. chromatography characterised by the separation mechanism
- B01D15/36—Selective adsorption, e.g. chromatography characterised by the separation mechanism involving ionic interaction
- B01D15/361—Ion-exchange
- B01D15/362—Cation-exchange
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01D—SEPARATION
- B01D15/00—Separating processes involving the treatment of liquids with solid sorbents; Apparatus therefor
- B01D15/08—Selective adsorption, e.g. chromatography
- B01D15/26—Selective adsorption, e.g. chromatography characterised by the separation mechanism
- B01D15/36—Selective adsorption, e.g. chromatography characterised by the separation mechanism involving ionic interaction
- B01D15/361—Ion-exchange
- B01D15/363—Anion-exchange
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Analytical Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Molecular Biology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Toxicology (AREA)
- Gastroenterology & Hepatology (AREA)
- Immunology (AREA)
- Cell Biology (AREA)
- Zoology (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Treatment Of Liquids With Adsorbents In General (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US07/857,022 US5252216A (en) | 1992-03-24 | 1992-03-24 | Protein purification |
PCT/US1993/002732 WO1993018835A1 (en) | 1992-03-24 | 1993-03-24 | Protein purification |
Publications (3)
Publication Number | Publication Date |
---|---|
NO943546D0 NO943546D0 (no) | 1994-09-23 |
NO943546L NO943546L (no) | 1994-11-23 |
NO310855B1 true NO310855B1 (no) | 2001-09-10 |
Family
ID=25324998
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
NO19943546A NO310855B1 (no) | 1992-03-24 | 1994-09-23 | Fremgangsmåte for rensing av protein |
Country Status (19)
Country | Link |
---|---|
US (1) | US5252216A (da) |
EP (1) | EP0643608B1 (da) |
JP (1) | JP3335629B2 (da) |
KR (1) | KR100241172B1 (da) |
AT (1) | ATE193839T1 (da) |
AU (1) | AU659936B2 (da) |
CA (1) | CA2132533C (da) |
DE (1) | DE69328864T2 (da) |
DK (1) | DK0643608T3 (da) |
ES (1) | ES2149206T3 (da) |
FI (1) | FI109202B (da) |
GR (1) | GR3034332T3 (da) |
MX (1) | MX9301655A (da) |
NO (1) | NO310855B1 (da) |
NZ (1) | NZ251601A (da) |
PT (1) | PT643608E (da) |
TW (1) | TW321651B (da) |
WO (1) | WO1993018835A1 (da) |
ZA (1) | ZA932015B (da) |
Families Citing this family (35)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US6395888B1 (en) * | 1996-02-01 | 2002-05-28 | Gilead Sciences, Inc. | High affinity nucleic acid ligands of complement system proteins |
DE4331358A1 (de) * | 1992-10-12 | 1994-04-14 | Braun Melsungen Ag | Verfahren zur quantitativen selektiven Entfernung oder präparativen Gewinnung von Tumor-Nekrose-Faktor (TNF) oder/und Lipopolysacchariden (LPS) aus wäßrigen Flüssigkeiten |
JPH08512323A (ja) * | 1993-07-09 | 1996-12-24 | スミスクライン・ビーチャム・コーポレイション | タンパク精製方法 |
US5679546A (en) * | 1993-09-24 | 1997-10-21 | Cytomed, Inc. | Chimeric proteins which block complement activation |
US5429746A (en) * | 1994-02-22 | 1995-07-04 | Smith Kline Beecham Corporation | Antibody purification |
DE19549420A1 (de) * | 1995-04-27 | 1997-09-18 | Braun Melsungen Ag | Verfahren zur simultanen extrakorporalen Elimination von Tumor-Nekrose Faktor alpha (TNF alpha) und bakteriellen Lipopolysacchariden (LPS) aus Vollblut oder/und Blutplasma |
EP1300679A3 (en) * | 1995-06-26 | 2004-04-14 | Perseptive Biosystems, Inc. | Molecular selection and analysis |
DE69627333T2 (de) * | 1995-06-26 | 2004-02-12 | PerSeptive Biosystems, Inc., Framingham | Automatisierte, kontinuierliche mehrdimensionale hochgeschwindigkeitsmolekularselektion und -analyse |
GB9515196D0 (en) * | 1995-07-25 | 1995-09-20 | Matthey Rustenburg Refines | Interseparation of platignum group metals |
JP2002511147A (ja) * | 1997-06-27 | 2002-04-09 | ライフ テクノロジーズ インク. | 生体分子の濃縮および精製のための一工程装置および方法 |
US5993653C1 (en) * | 1997-08-11 | 2001-11-06 | Phenomenex | Composition and column used in hplc |
US6869796B2 (en) * | 1997-08-26 | 2005-03-22 | Avaris Ab | Method of introducing organic molecules into target cells |
US20070122904A1 (en) * | 2000-09-29 | 2007-05-31 | Unisearch Limited | Method and apparatus for culturing cells |
US6855263B2 (en) * | 2002-07-23 | 2005-02-15 | Nuvue Technologies, Inc. | Rapid process for purification and concentration of plasmin |
DE10255508A1 (de) * | 2002-11-27 | 2004-06-17 | Forschungszentrum Jülich GmbH | Verfahren zur Kultivierung von Zellen zur Produktion von Substanzen |
US6913695B2 (en) * | 2003-07-08 | 2005-07-05 | Bayer Healthcare Llc | Sanitization of chromatographic media |
WO2005012349A2 (en) * | 2003-08-01 | 2005-02-10 | Lorantis Limited | Chromatographic process for the purification of notch ligands |
US7329353B2 (en) * | 2004-01-23 | 2008-02-12 | Amgen Inc. | LC/MS method of analyzing high molecular weight proteins |
US7803931B2 (en) | 2004-02-12 | 2010-09-28 | Archemix Corp. | Aptamer therapeutics useful in the treatment of complement-related disorders |
RU2426795C2 (ru) * | 2004-07-20 | 2011-08-20 | Симфоген А/С | Способ структурной характеристики рекомбинантного поликлонального белка или поликлональной клеточной линии |
US20090042274A1 (en) * | 2004-07-27 | 2009-02-12 | Genomidea Inc. | Method of Purifying Virus Envelope |
US8652334B2 (en) * | 2004-08-12 | 2014-02-18 | Lipoxen Technologies Limited | Fractionation of charged polysaccharide |
EP1738763A1 (en) | 2005-06-30 | 2007-01-03 | AVANT Immunotherapeutics, Inc. | Use of complement inhibitory proteins to treat spinal cord injury |
WO2007053235A1 (en) * | 2005-11-04 | 2007-05-10 | Sachem, Inc. | Cation-exchange displacement chromatography process and cationic organic compounds for use as displacer compounds in cation-exchange displacement chromatography process |
SI2596807T1 (sl) | 2006-03-08 | 2016-03-31 | Archemix Llc | Komplement vezavni aptameri in sredstva proti C5, uporabni pri zdravljenju očesnih motenj |
US20100222560A1 (en) | 2009-03-02 | 2010-09-02 | Zymo Research Corporation | Universal column |
KR102071834B1 (ko) | 2009-10-26 | 2020-01-30 | 에프. 호프만-라 로슈 아게 | 글리코실화된 면역글로불린의 제조 방법 |
CN103237557A (zh) | 2010-09-15 | 2013-08-07 | 赛尔戴克斯治疗公司 | 用可溶性I型补体受体(sCR1)治疗慢性肾病 |
WO2012048298A2 (en) | 2010-10-08 | 2012-04-12 | Caridianbct, Inc. | Methods and systems of growing and harvesting cells in a hollow fiber bioreactor system with control conditions |
CA2815237C (en) | 2010-10-27 | 2018-10-09 | Celldex Therapeutics, Inc. | Method of improving transplant function using soluble complement receptor type i (scr1) |
CN106715676A (zh) | 2014-09-26 | 2017-05-24 | 泰尔茂比司特公司 | 按计划供养 |
US11965175B2 (en) | 2016-05-25 | 2024-04-23 | Terumo Bct, Inc. | Cell expansion |
US11624046B2 (en) | 2017-03-31 | 2023-04-11 | Terumo Bct, Inc. | Cell expansion |
WO2018184028A2 (en) | 2017-03-31 | 2018-10-04 | Terumo Bct, Inc. | Cell expansion |
WO2023240322A1 (en) * | 2022-06-17 | 2023-12-21 | CSL Innovation Pty Ltd | Purification of soluble complement receptor and variants thereof |
Family Cites Families (15)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
DE2319495C2 (de) * | 1973-04-17 | 1985-01-10 | Yeda Research And Development Co., Ltd., Rehovot | Verfahren zum selektiven, reversiblen Binden von Biomolekülen an ein Adsorbens in einer chromatographischen Säule |
US4000098A (en) * | 1974-08-16 | 1976-12-28 | Palo Alto Medical Research Foundation | Separation of proteins by hydrophobic adsorption |
DE3149360A1 (de) * | 1981-12-12 | 1983-06-16 | Biotest-Serum-Institut Gmbh, 6000 Frankfurt | "verfahren zur reinigung und/oder phytohaemagglutinin-abtrennung von human-interleukin-2" |
US4920196A (en) * | 1982-07-30 | 1990-04-24 | Genentech, Inc. | Human lymphotoxin |
US4908434A (en) * | 1984-04-25 | 1990-03-13 | Sloan-Kettering Institute For Cancer Research | Process for preparing purified interleukin-2 |
US4743680A (en) * | 1985-02-01 | 1988-05-10 | New York University | Method for purifying antihemophilic factor |
US4894439A (en) * | 1986-05-22 | 1990-01-16 | Cetus Corporation | N-terminal derivatives of tumor necrosis factor purified by microporous PTFE membranes |
AU597924B2 (en) * | 1985-12-11 | 1990-06-14 | Natinco Nv | Solubilization of protein aggregates |
US4770781A (en) * | 1986-03-03 | 1988-09-13 | Merck & Co., Inc. | Purification of human interleukin-1 species |
US4771128A (en) * | 1986-10-10 | 1988-09-13 | Cetus Corporation | Method of purifying toxin conjugates using hydrophobic interaction chromatography |
AU609824B2 (en) * | 1987-06-15 | 1991-05-09 | Southern Cross Biotech Pty Ltd. | Production of proteins in active forms |
US4981799A (en) * | 1987-08-21 | 1991-01-01 | Takeda Chemical Industries, Ltd. | Acylamino acid racemase, production and use thereof |
US4765903A (en) * | 1987-10-06 | 1988-08-23 | Interferon Sciences, Inc. | Purification of monomeric interferon |
US5159063A (en) * | 1989-02-02 | 1992-10-27 | The United States Of America As Represented By The Department Of Health And Human Services | Isolation and characterization of a 120 kda glycoprotein plasma |
US5030352A (en) * | 1990-01-25 | 1991-07-09 | Purdue Research Foundation | Coated media for chromatography |
-
1992
- 1992-03-24 US US07/857,022 patent/US5252216A/en not_active Expired - Lifetime
-
1993
- 1993-03-22 ZA ZA932015A patent/ZA932015B/xx unknown
- 1993-03-24 WO PCT/US1993/002732 patent/WO1993018835A1/en active IP Right Grant
- 1993-03-24 DE DE69328864T patent/DE69328864T2/de not_active Expired - Fee Related
- 1993-03-24 DK DK93908538T patent/DK0643608T3/da active
- 1993-03-24 EP EP93908538A patent/EP0643608B1/en not_active Expired - Lifetime
- 1993-03-24 MX MX9301655A patent/MX9301655A/es unknown
- 1993-03-24 JP JP51681493A patent/JP3335629B2/ja not_active Expired - Fee Related
- 1993-03-24 KR KR1019940703342A patent/KR100241172B1/ko not_active IP Right Cessation
- 1993-03-24 CA CA002132533A patent/CA2132533C/en not_active Expired - Fee Related
- 1993-03-24 PT PT93908538T patent/PT643608E/pt unknown
- 1993-03-24 AT AT93908538T patent/ATE193839T1/de not_active IP Right Cessation
- 1993-03-24 AU AU39324/93A patent/AU659936B2/en not_active Ceased
- 1993-03-24 NZ NZ251601A patent/NZ251601A/en not_active IP Right Cessation
- 1993-03-24 ES ES93908538T patent/ES2149206T3/es not_active Expired - Lifetime
- 1993-07-27 TW TW082105986A patent/TW321651B/zh active
-
1994
- 1994-09-23 NO NO19943546A patent/NO310855B1/no unknown
- 1994-09-23 FI FI944412A patent/FI109202B/fi not_active IP Right Cessation
-
2000
- 2000-09-06 GR GR20000402020T patent/GR3034332T3/el not_active IP Right Cessation
Also Published As
Publication number | Publication date |
---|---|
CA2132533A1 (en) | 1993-09-30 |
ZA932015B (en) | 1994-09-21 |
EP0643608B1 (en) | 2000-06-14 |
ES2149206T3 (es) | 2000-11-01 |
NZ251601A (en) | 1997-03-24 |
FI109202B (fi) | 2002-06-14 |
GR3034332T3 (en) | 2000-12-29 |
PT643608E (pt) | 2000-11-30 |
CA2132533C (en) | 2004-01-13 |
WO1993018835A1 (en) | 1993-09-30 |
DE69328864T2 (de) | 2000-12-14 |
EP0643608A1 (en) | 1995-03-22 |
FI944412A0 (fi) | 1994-09-23 |
JPH07505469A (ja) | 1995-06-15 |
NO943546L (no) | 1994-11-23 |
ATE193839T1 (de) | 2000-06-15 |
EP0643608A4 (en) | 1997-11-26 |
DK0643608T3 (da) | 2000-10-02 |
KR100241172B1 (ko) | 2000-02-01 |
NO943546D0 (no) | 1994-09-23 |
KR950700779A (ko) | 1995-02-20 |
US5252216A (en) | 1993-10-12 |
AU3932493A (en) | 1993-10-21 |
DE69328864D1 (de) | 2000-07-20 |
TW321651B (da) | 1997-12-01 |
FI944412A (fi) | 1994-09-23 |
JP3335629B2 (ja) | 2002-10-21 |
AU659936B2 (en) | 1995-06-01 |
MX9301655A (es) | 1994-03-31 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
NO310855B1 (no) | Fremgangsmåte for rensing av protein | |
EP0812200B1 (en) | Protein purification | |
AU689552B2 (en) | Antibody purification | |
AU5545790A (en) | Process for purifying a protein | |
EP2102335B1 (en) | Purification of factor xi | |
CA2404155C (en) | Methods for purifying highly anionic proteins | |
EP4093755A1 (en) | Methods of purification | |
WO2023240322A1 (en) | Purification of soluble complement receptor and variants thereof |