KR960015399B1 - 면역 글로불린의 정제방법 - Google Patents
면역 글로불린의 정제방법 Download PDFInfo
- Publication number
- KR960015399B1 KR960015399B1 KR1019920701427A KR920701427A KR960015399B1 KR 960015399 B1 KR960015399 B1 KR 960015399B1 KR 1019920701427 A KR1019920701427 A KR 1019920701427A KR 920701427 A KR920701427 A KR 920701427A KR 960015399 B1 KR960015399 B1 KR 960015399B1
- Authority
- KR
- South Korea
- Prior art keywords
- antibody
- column
- protein
- compass
- cells
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Expired - Lifetime
Links
- 238000000034 method Methods 0.000 title claims description 38
- 108060003951 Immunoglobulin Proteins 0.000 title description 5
- 102000018358 immunoglobulin Human genes 0.000 title description 5
- 229940072221 immunoglobulins Drugs 0.000 title description 5
- 108090000623 proteins and genes Proteins 0.000 claims description 49
- 102000004169 proteins and genes Human genes 0.000 claims description 37
- 229920002684 Sepharose Polymers 0.000 claims description 12
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 claims description 9
- 230000007717 exclusion Effects 0.000 claims description 9
- 239000002245 particle Substances 0.000 claims description 8
- 238000002360 preparation method Methods 0.000 claims description 8
- 238000005342 ion exchange Methods 0.000 claims description 6
- 239000007864 aqueous solution Substances 0.000 claims description 5
- 238000000108 ultra-filtration Methods 0.000 claims description 4
- 101710120037 Toxin CcdB Proteins 0.000 claims description 3
- 230000002378 acidificating effect Effects 0.000 claims description 3
- 150000002500 ions Chemical class 0.000 claims description 3
- 239000003929 acidic solution Substances 0.000 claims description 2
- 238000005341 cation exchange Methods 0.000 claims description 2
- 238000012258 culturing Methods 0.000 claims description 2
- 239000012736 aqueous medium Substances 0.000 claims 4
- 210000004962 mammalian cell Anatomy 0.000 claims 1
- 210000004027 cell Anatomy 0.000 description 67
- 235000018102 proteins Nutrition 0.000 description 33
- 239000000203 mixture Substances 0.000 description 25
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 21
- 239000000499 gel Substances 0.000 description 18
- 238000009472 formulation Methods 0.000 description 16
- 101150074155 DHFR gene Proteins 0.000 description 15
- 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 14
- 239000000427 antigen Substances 0.000 description 14
- 108091007433 antigens Proteins 0.000 description 14
- 102000036639 antigens Human genes 0.000 description 14
- 229960000485 methotrexate Drugs 0.000 description 14
- 239000000523 sample Substances 0.000 description 14
- 239000002609 medium Substances 0.000 description 13
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 12
- FDGQSTZJBFJUBT-UHFFFAOYSA-N hypoxanthine Chemical compound O=C1NC=NC2=C1NC=N2 FDGQSTZJBFJUBT-UHFFFAOYSA-N 0.000 description 12
- 239000012071 phase Substances 0.000 description 12
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 12
- 230000005526 G1 to G0 transition Effects 0.000 description 11
- IQFYYKKMVGJFEH-XLPZGREQSA-N Thymidine Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](CO)[C@@H](O)C1 IQFYYKKMVGJFEH-XLPZGREQSA-N 0.000 description 10
- 239000002299 complementary DNA Substances 0.000 description 10
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 10
- 239000002953 phosphate buffered saline Substances 0.000 description 10
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 9
- 241000282414 Homo sapiens Species 0.000 description 9
- 230000000694 effects Effects 0.000 description 9
- 239000002158 endotoxin Substances 0.000 description 9
- 239000000463 material Substances 0.000 description 9
- BDAGIHXWWSANSR-UHFFFAOYSA-N methanoic acid Natural products OC=O BDAGIHXWWSANSR-UHFFFAOYSA-N 0.000 description 9
- 238000003199 nucleic acid amplification method Methods 0.000 description 9
- 238000004007 reversed phase HPLC Methods 0.000 description 9
- 239000012505 Superdex™ Substances 0.000 description 8
- 230000003321 amplification Effects 0.000 description 8
- 239000000872 buffer Substances 0.000 description 8
- 210000002966 serum Anatomy 0.000 description 8
- 239000000243 solution Substances 0.000 description 8
- 239000002202 Polyethylene glycol Substances 0.000 description 7
- 239000012634 fragment Substances 0.000 description 7
- 229940027941 immunoglobulin g Drugs 0.000 description 7
- 229920001223 polyethylene glycol Polymers 0.000 description 7
- 238000002965 ELISA Methods 0.000 description 6
- UGQMRVRMYYASKQ-UHFFFAOYSA-N Hypoxanthine nucleoside Natural products OC1C(O)C(CO)OC1N1C(NC=NC2=O)=C2N=C1 UGQMRVRMYYASKQ-UHFFFAOYSA-N 0.000 description 6
- 201000010099 disease Diseases 0.000 description 6
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 6
- 238000010828 elution Methods 0.000 description 6
- 239000012528 membrane Substances 0.000 description 6
- 238000000746 purification Methods 0.000 description 6
- 238000000926 separation method Methods 0.000 description 6
- 102000007469 Actins Human genes 0.000 description 5
- 108010085238 Actins Proteins 0.000 description 5
- CIWBSHSKHKDKBQ-JLAZNSOCSA-N Ascorbic acid Chemical compound OC[C@H](O)[C@H]1OC(=O)C(O)=C1O CIWBSHSKHKDKBQ-JLAZNSOCSA-N 0.000 description 5
- DWRXFEITVBNRMK-UHFFFAOYSA-N Beta-D-1-Arabinofuranosylthymine Natural products O=C1NC(=O)C(C)=CN1C1C(O)C(O)C(CO)O1 DWRXFEITVBNRMK-UHFFFAOYSA-N 0.000 description 5
- 108020004414 DNA Proteins 0.000 description 5
- 229930193140 Neomycin Natural products 0.000 description 5
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 5
- 238000004458 analytical method Methods 0.000 description 5
- 238000003556 assay Methods 0.000 description 5
- IQFYYKKMVGJFEH-UHFFFAOYSA-N beta-L-thymidine Natural products O=C1NC(=O)C(C)=CN1C1OC(CO)C(O)C1 IQFYYKKMVGJFEH-UHFFFAOYSA-N 0.000 description 5
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 5
- 238000010367 cloning Methods 0.000 description 5
- 239000001963 growth medium Substances 0.000 description 5
- 229960004927 neomycin Drugs 0.000 description 5
- 239000011148 porous material Substances 0.000 description 5
- 230000008569 process Effects 0.000 description 5
- 229940104230 thymidine Drugs 0.000 description 5
- JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-UHFFFAOYSA-N 0.000 description 4
- OSWFIVFLDKOXQC-UHFFFAOYSA-N 4-(3-methoxyphenyl)aniline Chemical compound COC1=CC=CC(C=2C=CC(N)=CC=2)=C1 OSWFIVFLDKOXQC-UHFFFAOYSA-N 0.000 description 4
- 102000004190 Enzymes Human genes 0.000 description 4
- 108090000790 Enzymes Proteins 0.000 description 4
- 239000002253 acid Substances 0.000 description 4
- 230000000295 complement effect Effects 0.000 description 4
- 235000019253 formic acid Nutrition 0.000 description 4
- 125000000524 functional group Chemical group 0.000 description 4
- 230000028993 immune response Effects 0.000 description 4
- 238000001802 infusion Methods 0.000 description 4
- NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 description 4
- 210000004698 lymphocyte Anatomy 0.000 description 4
- 238000004519 manufacturing process Methods 0.000 description 4
- 229920000642 polymer Polymers 0.000 description 4
- 239000000047 product Substances 0.000 description 4
- LXNHXLLTXMVWPM-UHFFFAOYSA-N pyridoxine Chemical compound CC1=NC=C(CO)C(CO)=C1O LXNHXLLTXMVWPM-UHFFFAOYSA-N 0.000 description 4
- 238000001542 size-exclusion chromatography Methods 0.000 description 4
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 4
- 239000013598 vector Substances 0.000 description 4
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 3
- 229920000936 Agarose Polymers 0.000 description 3
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 3
- 108020004705 Codon Proteins 0.000 description 3
- 241000699670 Mus sp. Species 0.000 description 3
- 239000001888 Peptone Substances 0.000 description 3
- 108010080698 Peptones Proteins 0.000 description 3
- 206010035226 Plasma cell myeloma Diseases 0.000 description 3
- 241000700159 Rattus Species 0.000 description 3
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 3
- 238000002835 absorbance Methods 0.000 description 3
- 150000001413 amino acids Chemical group 0.000 description 3
- 150000001768 cations Chemical class 0.000 description 3
- 238000004587 chromatography analysis Methods 0.000 description 3
- 239000000356 contaminant Substances 0.000 description 3
- 239000003814 drug Substances 0.000 description 3
- 239000012091 fetal bovine serum Substances 0.000 description 3
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 3
- 239000000178 monomer Substances 0.000 description 3
- 201000000050 myeloid neoplasm Diseases 0.000 description 3
- 108020004707 nucleic acids Proteins 0.000 description 3
- 102000039446 nucleic acids Human genes 0.000 description 3
- 150000007523 nucleic acids Chemical class 0.000 description 3
- 235000019319 peptone Nutrition 0.000 description 3
- 230000008488 polyadenylation Effects 0.000 description 3
- 230000035755 proliferation Effects 0.000 description 3
- 239000011780 sodium chloride Substances 0.000 description 3
- 239000006228 supernatant Substances 0.000 description 3
- 230000001225 therapeutic effect Effects 0.000 description 3
- 210000001519 tissue Anatomy 0.000 description 3
- MYRTYDVEIRVNKP-UHFFFAOYSA-N 1,2-Divinylbenzene Chemical compound C=CC1=CC=CC=C1C=C MYRTYDVEIRVNKP-UHFFFAOYSA-N 0.000 description 2
- IIZPXYDJLKNOIY-JXPKJXOSSA-N 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine Chemical compound CCCCCCCCCCCCCCCC(=O)OC[C@H](COP([O-])(=O)OCC[N+](C)(C)C)OC(=O)CCC\C=C/C\C=C/C\C=C/C\C=C/CCCCC IIZPXYDJLKNOIY-JXPKJXOSSA-N 0.000 description 2
- HZAXFHJVJLSVMW-UHFFFAOYSA-N 2-Aminoethan-1-ol Chemical compound NCCO HZAXFHJVJLSVMW-UHFFFAOYSA-N 0.000 description 2
- 208000014644 Brain disease Diseases 0.000 description 2
- 241000283707 Capra Species 0.000 description 2
- 102100035360 Cerebellar degeneration-related antigen 1 Human genes 0.000 description 2
- 108020004635 Complementary DNA Proteins 0.000 description 2
- RGHNJXZEOKUKBD-SQOUGZDYSA-M D-gluconate Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C([O-])=O RGHNJXZEOKUKBD-SQOUGZDYSA-M 0.000 description 2
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- 238000011993 High Performance Size Exclusion Chromatography Methods 0.000 description 2
- 241000282412 Homo Species 0.000 description 2
- 101000756632 Homo sapiens Actin, cytoplasmic 1 Proteins 0.000 description 2
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 2
- 102000004877 Insulin Human genes 0.000 description 2
- 108090001061 Insulin Proteins 0.000 description 2
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 2
- 239000002211 L-ascorbic acid Substances 0.000 description 2
- 235000000069 L-ascorbic acid Nutrition 0.000 description 2
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 2
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 2
- 241001465754 Metazoa Species 0.000 description 2
- 241000699666 Mus <mouse, genus> Species 0.000 description 2
- 208000015914 Non-Hodgkin lymphomas Diseases 0.000 description 2
- 108091034117 Oligonucleotide Proteins 0.000 description 2
- 229910019142 PO4 Inorganic materials 0.000 description 2
- 102000003992 Peroxidases Human genes 0.000 description 2
- 108010040201 Polymyxins Proteins 0.000 description 2
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 2
- 101000702488 Rattus norvegicus High affinity cationic amino acid transporter 1 Proteins 0.000 description 2
- PMZURENOXWZQFD-UHFFFAOYSA-L Sodium Sulfate Chemical compound [Na+].[Na+].[O-]S([O-])(=O)=O PMZURENOXWZQFD-UHFFFAOYSA-L 0.000 description 2
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 2
- 239000004473 Threonine Substances 0.000 description 2
- 102000004338 Transferrin Human genes 0.000 description 2
- 108090000901 Transferrin Proteins 0.000 description 2
- DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 2
- 239000007983 Tris buffer Substances 0.000 description 2
- 241000700605 Viruses Species 0.000 description 2
- 229930003779 Vitamin B12 Natural products 0.000 description 2
- 239000003242 anti bacterial agent Substances 0.000 description 2
- 229940088710 antibiotic agent Drugs 0.000 description 2
- 229960005070 ascorbic acid Drugs 0.000 description 2
- 238000003776 cleavage reaction Methods 0.000 description 2
- FDJOLVPMNUYSCM-WZHZPDAFSA-L cobalt(3+);[(2r,3s,4r,5s)-5-(5,6-dimethylbenzimidazol-1-yl)-4-hydroxy-2-(hydroxymethyl)oxolan-3-yl] [(2r)-1-[3-[(1r,2r,3r,4z,7s,9z,12s,13s,14z,17s,18s,19r)-2,13,18-tris(2-amino-2-oxoethyl)-7,12,17-tris(3-amino-3-oxopropyl)-3,5,8,8,13,15,18,19-octamethyl-2 Chemical compound [Co+3].N#[C-].N([C@@H]([C@]1(C)[N-]\C([C@H]([C@@]1(CC(N)=O)C)CCC(N)=O)=C(\C)/C1=N/C([C@H]([C@@]1(CC(N)=O)C)CCC(N)=O)=C\C1=N\C([C@H](C1(C)C)CCC(N)=O)=C/1C)[C@@H]2CC(N)=O)=C\1[C@]2(C)CCC(=O)NC[C@@H](C)OP([O-])(=O)O[C@H]1[C@@H](O)[C@@H](N2C3=CC(C)=C(C)C=C3N=C2)O[C@@H]1CO FDJOLVPMNUYSCM-WZHZPDAFSA-L 0.000 description 2
- 238000010790 dilution Methods 0.000 description 2
- 239000012895 dilution Substances 0.000 description 2
- 238000004090 dissolution Methods 0.000 description 2
- 239000012153 distilled water Substances 0.000 description 2
- 229940079593 drug Drugs 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 238000001914 filtration Methods 0.000 description 2
- 229940014144 folate Drugs 0.000 description 2
- OVBPIULPVIDEAO-LBPRGKRZSA-N folic acid Chemical compound C=1N=C2NC(N)=NC(=O)C2=NC=1CNC1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 OVBPIULPVIDEAO-LBPRGKRZSA-N 0.000 description 2
- 235000019152 folic acid Nutrition 0.000 description 2
- 239000011724 folic acid Substances 0.000 description 2
- 229940050410 gluconate Drugs 0.000 description 2
- PJJJBBJSCAKJQF-UHFFFAOYSA-N guanidinium chloride Chemical compound [Cl-].NC(N)=[NH2+] PJJJBBJSCAKJQF-UHFFFAOYSA-N 0.000 description 2
- 238000004128 high performance liquid chromatography Methods 0.000 description 2
- 210000004408 hybridoma Anatomy 0.000 description 2
- 238000011534 incubation Methods 0.000 description 2
- 229940125396 insulin Drugs 0.000 description 2
- 150000002605 large molecules Chemical class 0.000 description 2
- 239000000787 lecithin Substances 0.000 description 2
- 229940067606 lecithin Drugs 0.000 description 2
- 235000010445 lecithin Nutrition 0.000 description 2
- 239000003446 ligand Substances 0.000 description 2
- 238000012454 limulus amebocyte lysate test Methods 0.000 description 2
- 229920002521 macromolecule Polymers 0.000 description 2
- 239000003550 marker Substances 0.000 description 2
- 229930182817 methionine Natural products 0.000 description 2
- SXTAYKAGBXMACB-UHFFFAOYSA-N methionine sulfoximine Chemical compound CS(=N)(=O)CCC(N)C(O)=O SXTAYKAGBXMACB-UHFFFAOYSA-N 0.000 description 2
- 230000003287 optical effect Effects 0.000 description 2
- 108040007629 peroxidase activity proteins Proteins 0.000 description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 2
- 239000010452 phosphate Substances 0.000 description 2
- 239000002504 physiological saline solution Substances 0.000 description 2
- 229920002401 polyacrylamide Polymers 0.000 description 2
- 229920001184 polypeptide Polymers 0.000 description 2
- 108090000765 processed proteins & peptides Proteins 0.000 description 2
- 102000004196 processed proteins & peptides Human genes 0.000 description 2
- 230000000644 propagated effect Effects 0.000 description 2
- KIDHWZJUCRJVML-UHFFFAOYSA-N putrescine Chemical compound NCCCCN KIDHWZJUCRJVML-UHFFFAOYSA-N 0.000 description 2
- RADKZDMFGJYCBB-UHFFFAOYSA-N pyridoxal hydrochloride Natural products CC1=NC=C(CO)C(C=O)=C1O RADKZDMFGJYCBB-UHFFFAOYSA-N 0.000 description 2
- 238000011084 recovery Methods 0.000 description 2
- 230000009467 reduction Effects 0.000 description 2
- 230000007017 scission Effects 0.000 description 2
- 239000012679 serum free medium Substances 0.000 description 2
- 150000003384 small molecules Chemical class 0.000 description 2
- 239000011734 sodium Substances 0.000 description 2
- 241000894007 species Species 0.000 description 2
- 125000003396 thiol group Chemical group [H]S* 0.000 description 2
- 239000003104 tissue culture media Substances 0.000 description 2
- 239000012581 transferrin Substances 0.000 description 2
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 2
- 239000013621 viresolve pro solution Substances 0.000 description 2
- 230000003612 virological effect Effects 0.000 description 2
- 235000019163 vitamin B12 Nutrition 0.000 description 2
- 239000011715 vitamin B12 Substances 0.000 description 2
- 235000019158 vitamin B6 Nutrition 0.000 description 2
- 239000011726 vitamin B6 Substances 0.000 description 2
- 229940011671 vitamin b6 Drugs 0.000 description 2
- 239000001149 (9Z,12Z)-octadeca-9,12-dienoate Substances 0.000 description 1
- WTTJVINHCBCLGX-UHFFFAOYSA-N (9trans,12cis)-methyl linoleate Natural products CCCCCC=CCC=CCCCCCCCC(=O)OC WTTJVINHCBCLGX-UHFFFAOYSA-N 0.000 description 1
- FCWXSQNGFGSDMO-UHFFFAOYSA-N 2-iodoacetamide;2-iodoacetic acid Chemical compound NC(=O)CI.OC(=O)CI FCWXSQNGFGSDMO-UHFFFAOYSA-N 0.000 description 1
- LNJCGNRKWOHFFV-UHFFFAOYSA-N 3-(2-hydroxyethylsulfanyl)propanenitrile Chemical compound OCCSCCC#N LNJCGNRKWOHFFV-UHFFFAOYSA-N 0.000 description 1
- PMJHNEFCWLUZBC-UHFFFAOYSA-N 4-(4-amino-3-methylphenyl)-2,6,6-trimethylcyclohexa-1,3-dien-1-amine Chemical compound CC1=C(N)C(C)(C)CC(C=2C=C(C)C(N)=CC=2)=C1 PMJHNEFCWLUZBC-UHFFFAOYSA-N 0.000 description 1
- 206010002199 Anaphylactic shock Diseases 0.000 description 1
- 208000023275 Autoimmune disease Diseases 0.000 description 1
- 208000028564 B-cell non-Hodgkin lymphoma Diseases 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 102100024217 CAMPATH-1 antigen Human genes 0.000 description 1
- 108010047041 Complementarity Determining Regions Proteins 0.000 description 1
- 241000699802 Cricetulus griseus Species 0.000 description 1
- 229920002307 Dextran Polymers 0.000 description 1
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 1
- 108060002716 Exonuclease Proteins 0.000 description 1
- 102000009109 Fc receptors Human genes 0.000 description 1
- 108010087819 Fc receptors Proteins 0.000 description 1
- 229920006358 Fluon Polymers 0.000 description 1
- 101150074355 GS gene Proteins 0.000 description 1
- 108010010803 Gelatin Proteins 0.000 description 1
- 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 1
- 239000004471 Glycine Substances 0.000 description 1
- 239000007995 HEPES buffer Substances 0.000 description 1
- 101000980814 Homo sapiens CAMPATH-1 antigen Proteins 0.000 description 1
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 1
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 1
- 102000018071 Immunoglobulin Fc Fragments Human genes 0.000 description 1
- 108010091135 Immunoglobulin Fc Fragments Proteins 0.000 description 1
- 102000003960 Ligases Human genes 0.000 description 1
- 108090000364 Ligases Proteins 0.000 description 1
- 241000239218 Limulus Species 0.000 description 1
- PKIXXJPMNDDDOS-UHFFFAOYSA-N Methyl linoleate Natural products CCCCC=CCCC=CCCCCCCCC(=O)OC PKIXXJPMNDDDOS-UHFFFAOYSA-N 0.000 description 1
- 108091007491 NSP3 Papain-like protease domains Proteins 0.000 description 1
- 206010028980 Neoplasm Diseases 0.000 description 1
- 238000000636 Northern blotting Methods 0.000 description 1
- 108090000295 Nucellin Proteins 0.000 description 1
- 108091028043 Nucleic acid sequence Proteins 0.000 description 1
- 239000004677 Nylon Substances 0.000 description 1
- 229920002302 Nylon 6,6 Polymers 0.000 description 1
- 102000045595 Phosphoprotein Phosphatases Human genes 0.000 description 1
- 108700019535 Phosphoprotein Phosphatases Proteins 0.000 description 1
- 102000004160 Phosphoric Monoester Hydrolases Human genes 0.000 description 1
- 108090000608 Phosphoric Monoester Hydrolases Proteins 0.000 description 1
- 239000004793 Polystyrene Substances 0.000 description 1
- 201000004681 Psoriasis Diseases 0.000 description 1
- 239000005700 Putrescine Substances 0.000 description 1
- 241000283984 Rodentia Species 0.000 description 1
- 108010071390 Serum Albumin Proteins 0.000 description 1
- 102000007562 Serum Albumin Human genes 0.000 description 1
- 208000021386 Sjogren Syndrome Diseases 0.000 description 1
- 241000191967 Staphylococcus aureus Species 0.000 description 1
- 108091081024 Start codon Proteins 0.000 description 1
- QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 description 1
- 210000001744 T-lymphocyte Anatomy 0.000 description 1
- 108010022394 Threonine synthase Proteins 0.000 description 1
- 206010052779 Transplant rejections Diseases 0.000 description 1
- 102000004142 Trypsin Human genes 0.000 description 1
- 108090000631 Trypsin Proteins 0.000 description 1
- 206010047115 Vasculitis Diseases 0.000 description 1
- ZXKIFUWANBZSKF-UHFFFAOYSA-N [I].CC(O)=O Chemical compound [I].CC(O)=O ZXKIFUWANBZSKF-UHFFFAOYSA-N 0.000 description 1
- 239000004480 active ingredient Substances 0.000 description 1
- 230000006978 adaptation Effects 0.000 description 1
- 239000011543 agarose gel Substances 0.000 description 1
- 230000029936 alkylation Effects 0.000 description 1
- 238000005804 alkylation reaction Methods 0.000 description 1
- 235000001014 amino acid Nutrition 0.000 description 1
- 208000003455 anaphylaxis Diseases 0.000 description 1
- 150000001450 anions Chemical class 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 239000012062 aqueous buffer Substances 0.000 description 1
- 208000006673 asthma Diseases 0.000 description 1
- 230000002238 attenuated effect Effects 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 239000011324 bead Substances 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 1
- 238000004166 bioassay 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
- 210000001772 blood platelet Anatomy 0.000 description 1
- 210000002798 bone marrow cell Anatomy 0.000 description 1
- 239000007975 buffered saline Substances 0.000 description 1
- 239000001506 calcium phosphate Substances 0.000 description 1
- 229910000389 calcium phosphate Inorganic materials 0.000 description 1
- 235000011010 calcium phosphates Nutrition 0.000 description 1
- 150000001720 carbohydrates Chemical class 0.000 description 1
- 235000014633 carbohydrates Nutrition 0.000 description 1
- 229910002091 carbon monoxide Inorganic materials 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- 239000005018 casein Substances 0.000 description 1
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 1
- 235000021240 caseins Nutrition 0.000 description 1
- 230000006037 cell lysis Effects 0.000 description 1
- 239000006285 cell suspension Substances 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 238000012761 co-transfection Methods 0.000 description 1
- 239000002131 composite material Substances 0.000 description 1
- 238000007906 compression Methods 0.000 description 1
- 230000006835 compression Effects 0.000 description 1
- 238000011109 contamination Methods 0.000 description 1
- 229910000365 copper sulfate Inorganic materials 0.000 description 1
- ARUVKPQLZAKDPS-UHFFFAOYSA-L copper(II) sulfate Chemical compound [Cu+2].[O-][S+2]([O-])([O-])[O-] ARUVKPQLZAKDPS-UHFFFAOYSA-L 0.000 description 1
- 230000008878 coupling Effects 0.000 description 1
- 238000010168 coupling process Methods 0.000 description 1
- 238000005859 coupling reaction Methods 0.000 description 1
- 239000013078 crystal Substances 0.000 description 1
- 239000012228 culture supernatant Substances 0.000 description 1
- 230000009089 cytolysis Effects 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 239000003599 detergent Substances 0.000 description 1
- 206010012601 diabetes mellitus Diseases 0.000 description 1
- 238000000502 dialysis Methods 0.000 description 1
- 235000005911 diet Nutrition 0.000 description 1
- 230000037213 diet Effects 0.000 description 1
- 102000004419 dihydrofolate reductase Human genes 0.000 description 1
- 239000003085 diluting agent Substances 0.000 description 1
- AIUDWMLXCFRVDR-UHFFFAOYSA-N dimethyl 2-(3-ethyl-3-methylpentyl)propanedioate Chemical compound CCC(C)(CC)CCC(C(=O)OC)C(=O)OC AIUDWMLXCFRVDR-UHFFFAOYSA-N 0.000 description 1
- 150000002009 diols Chemical group 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
- 229910000397 disodium phosphate Inorganic materials 0.000 description 1
- 235000019800 disodium phosphate Nutrition 0.000 description 1
- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 1
- 230000009977 dual effect Effects 0.000 description 1
- 239000012636 effector Substances 0.000 description 1
- 230000005684 electric field Effects 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 108010072542 endotoxin binding proteins Proteins 0.000 description 1
- 239000003623 enhancer Substances 0.000 description 1
- 210000003743 erythrocyte Anatomy 0.000 description 1
- 239000003797 essential amino acid Substances 0.000 description 1
- 235000020776 essential amino acid Nutrition 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 102000013165 exonuclease Human genes 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 229960002413 ferric citrate Drugs 0.000 description 1
- 230000001605 fetal effect Effects 0.000 description 1
- 239000012467 final product Substances 0.000 description 1
- 239000012737 fresh medium Substances 0.000 description 1
- 239000007789 gas Substances 0.000 description 1
- 239000008273 gelatin Substances 0.000 description 1
- 229920000159 gelatin Polymers 0.000 description 1
- 235000019322 gelatine Nutrition 0.000 description 1
- 235000011852 gelatine desserts Nutrition 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 239000011544 gradient gel Substances 0.000 description 1
- 210000003714 granulocyte Anatomy 0.000 description 1
- 210000004524 haematopoietic cell Anatomy 0.000 description 1
- 230000003053 immunization Effects 0.000 description 1
- 238000002649 immunization Methods 0.000 description 1
- 238000003018 immunoassay Methods 0.000 description 1
- 230000001506 immunosuppresive effect Effects 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 239000012678 infectious agent Substances 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 238000007918 intramuscular administration Methods 0.000 description 1
- 238000007912 intraperitoneal administration Methods 0.000 description 1
- 238000001990 intravenous administration Methods 0.000 description 1
- 238000004255 ion exchange chromatography Methods 0.000 description 1
- NPFOYSMITVOQOS-UHFFFAOYSA-K iron(III) citrate Chemical compound [Fe+3].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O NPFOYSMITVOQOS-UHFFFAOYSA-K 0.000 description 1
- 239000010410 layer Substances 0.000 description 1
- 208000032839 leukemia Diseases 0.000 description 1
- 150000002632 lipids Chemical class 0.000 description 1
- AGBQKNBQESQNJD-UHFFFAOYSA-M lipoate Chemical compound [O-]C(=O)CCCCC1CCSS1 AGBQKNBQESQNJD-UHFFFAOYSA-M 0.000 description 1
- 235000019136 lipoic acid Nutrition 0.000 description 1
- 206010025135 lupus erythematosus Diseases 0.000 description 1
- 230000003211 malignant effect Effects 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 238000001471 micro-filtration Methods 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 238000013508 migration Methods 0.000 description 1
- 230000005012 migration Effects 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 238000012544 monitoring process Methods 0.000 description 1
- 201000006417 multiple sclerosis Diseases 0.000 description 1
- 231100000417 nephrotoxicity Toxicity 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- 229920001778 nylon Polymers 0.000 description 1
- 229920000620 organic polymer Polymers 0.000 description 1
- 239000003960 organic solvent Substances 0.000 description 1
- 229940043515 other immunoglobulins in atc Drugs 0.000 description 1
- 210000001672 ovary Anatomy 0.000 description 1
- 244000052769 pathogen Species 0.000 description 1
- 230000037361 pathway Effects 0.000 description 1
- 239000012466 permeate Substances 0.000 description 1
- 229920003023 plastic Polymers 0.000 description 1
- 239000004033 plastic Substances 0.000 description 1
- 229920002223 polystyrene Polymers 0.000 description 1
- OTYBMLCTZGSZBG-UHFFFAOYSA-L potassium sulfate Chemical compound [K+].[K+].[O-]S([O-])(=O)=O OTYBMLCTZGSZBG-UHFFFAOYSA-L 0.000 description 1
- 229910052939 potassium sulfate Inorganic materials 0.000 description 1
- 239000001120 potassium sulphate Substances 0.000 description 1
- 235000011151 potassium sulphates Nutrition 0.000 description 1
- 239000012460 protein solution Substances 0.000 description 1
- 238000003908 quality control method Methods 0.000 description 1
- 238000003259 recombinant expression Methods 0.000 description 1
- 238000002407 reforming Methods 0.000 description 1
- 239000004627 regenerated cellulose Substances 0.000 description 1
- 230000010076 replication Effects 0.000 description 1
- 230000004044 response Effects 0.000 description 1
- 108091008146 restriction endonucleases Proteins 0.000 description 1
- 206010039073 rheumatoid arthritis Diseases 0.000 description 1
- 239000012488 sample solution Substances 0.000 description 1
- 238000012216 screening Methods 0.000 description 1
- 238000010187 selection method Methods 0.000 description 1
- 230000035945 sensitivity Effects 0.000 description 1
- 239000000741 silica gel Substances 0.000 description 1
- 229910002027 silica gel Inorganic materials 0.000 description 1
- 239000000377 silicon dioxide Substances 0.000 description 1
- 239000002356 single layer Substances 0.000 description 1
- PXLIDIMHPNPGMH-UHFFFAOYSA-N sodium chromate Chemical compound [Na+].[Na+].[O-][Cr]([O-])(=O)=O PXLIDIMHPNPGMH-UHFFFAOYSA-N 0.000 description 1
- 229910052938 sodium sulfate Inorganic materials 0.000 description 1
- 235000011152 sodium sulphate Nutrition 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 229910001220 stainless steel Inorganic materials 0.000 description 1
- 239000010935 stainless steel Substances 0.000 description 1
- 230000001954 sterilising effect Effects 0.000 description 1
- 238000004659 sterilization and disinfection Methods 0.000 description 1
- 238000007920 subcutaneous administration Methods 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 229910021653 sulphate ion Inorganic materials 0.000 description 1
- 239000013589 supplement Substances 0.000 description 1
- 230000009885 systemic effect Effects 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 229960002663 thioctic acid Drugs 0.000 description 1
- 210000001685 thyroid gland Anatomy 0.000 description 1
- 238000012250 transgenic expression Methods 0.000 description 1
- 238000002054 transplantation Methods 0.000 description 1
- QORWJWZARLRLPR-UHFFFAOYSA-H tricalcium bis(phosphate) Chemical compound [Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O QORWJWZARLRLPR-UHFFFAOYSA-H 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
- 239000003656 tris buffered saline Substances 0.000 description 1
- 239000012588 trypsin Substances 0.000 description 1
- 238000000825 ultraviolet detection Methods 0.000 description 1
- 230000035899 viability Effects 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- NWONKYPBYAMBJT-UHFFFAOYSA-L zinc sulfate Chemical compound [Zn+2].[O-]S([O-])(=O)=O NWONKYPBYAMBJT-UHFFFAOYSA-L 0.000 description 1
- 229910000368 zinc sulfate Inorganic materials 0.000 description 1
- 229960001763 zinc sulfate Drugs 0.000 description 1
Classifications
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/395—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/06—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies from serum
- C07K16/065—Purification, fragmentation
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
- C07K16/2893—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against CD52
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/24—Immunoglobulins specific features characterized by taxonomic origin containing regions, domains or residues from different species, e.g. chimeric, humanized or veneered
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/70—Fusion polypeptide containing domain for protein-protein interaction
- C07K2319/74—Fusion polypeptide containing domain for protein-protein interaction containing a fusion for binding to a cell surface receptor
- C07K2319/75—Fusion polypeptide containing domain for protein-protein interaction containing a fusion for binding to a cell surface receptor containing a fusion for activation of a cell surface receptor, e.g. thrombopoeitin, NPY and other peptide hormones
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Immunology (AREA)
- Medicinal Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Mycology (AREA)
- Veterinary Medicine (AREA)
- Microbiology (AREA)
- Animal Behavior & Ethology (AREA)
- Epidemiology (AREA)
- Pharmacology & Pharmacy (AREA)
- Public Health (AREA)
- Engineering & Computer Science (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Steroid Compounds (AREA)
- Saccharide Compounds (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GB9022547.5 | 1990-10-17 | ||
| GB909022547A GB9022547D0 (en) | 1990-10-17 | 1990-10-17 | Purified immunoglobulin |
| PCT/GB1991/001816 WO1992007084A1 (en) | 1990-10-17 | 1991-10-17 | Purified cdw52-specific antibodies |
Related Child Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| KR1019920702699A Division KR100193314B1 (ko) | 1990-10-17 | 1992-10-30 | 정제된 면역 글로불린 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| KR920703108A KR920703108A (ko) | 1992-12-17 |
| KR960015399B1 true KR960015399B1 (ko) | 1996-11-13 |
Family
ID=10683866
Family Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| KR1019920701427A Expired - Lifetime KR960015399B1 (ko) | 1990-10-17 | 1991-10-17 | 면역 글로불린의 정제방법 |
| KR1019920702699A Expired - Lifetime KR100193314B1 (ko) | 1990-10-17 | 1992-10-30 | 정제된 면역 글로불린 |
Family Applications After (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| KR1019920702699A Expired - Lifetime KR100193314B1 (ko) | 1990-10-17 | 1992-10-30 | 정제된 면역 글로불린 |
Country Status (29)
Families Citing this family (56)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB9022545D0 (en) | 1990-10-17 | 1990-11-28 | Wellcome Found | Culture medium |
| IL103418A (en) * | 1991-10-15 | 1997-11-20 | Wellcome Found | Therapeutic agent for the t-cell mediated inflammation of the joints and its production |
| GB9125768D0 (en) * | 1991-12-04 | 1992-02-05 | Hale Geoffrey | Therapeutic method |
| GB9300501D0 (en) * | 1993-01-09 | 1993-03-03 | Wellcome Found | Purification of immunoglobulin |
| NZ315357A (en) † | 1995-08-01 | 1999-08-30 | Pasteur Merieux Serums Vacc | Method for industrially producing a japanese encephalitis vaccine, and resulting vaccine |
| US6090382A (en) * | 1996-02-09 | 2000-07-18 | Basf Aktiengesellschaft | Human antibodies that bind human TNFα |
| WO1997029131A1 (en) * | 1996-02-09 | 1997-08-14 | Basf Aktiengesellschaft | HUMAN ANTIBODIES THAT BIND HUMAN TNF$g(a) |
| GB9603256D0 (en) * | 1996-02-16 | 1996-04-17 | Wellcome Found | Antibodies |
| US20030023043A1 (en) * | 2000-03-02 | 2003-01-30 | Kazuhisa Uchida | Method of separating and purifying protein |
| EP2336149A1 (en) | 2001-03-09 | 2011-06-22 | Chugai Seiyaku Kabushiki Kaisha | Protein purification method |
| JP4288153B2 (ja) * | 2001-06-05 | 2009-07-01 | ジェネティクス インスティテュート，エルエルシー | 非常に陰イオン性であるタンパク質を精製する方法 |
| GB0220894D0 (en) * | 2002-09-09 | 2002-10-16 | Millipore Uk Ltd | Method of separation |
| EP1561756B1 (en) | 2002-09-11 | 2015-12-23 | Chugai Seiyaku Kabushiki Kaisha | Method of purifying protein |
| EP2314604A3 (en) | 2002-10-15 | 2011-05-25 | Intercell AG | Nucleic acids coding for adhesion factors of group B streptococcus, adhesion factors of group B streptococcus and further uses thereof |
| GB0304576D0 (en) * | 2003-02-28 | 2003-04-02 | Lonza Biologics Plc | Protein a chromatography |
| BRPI0417993A (pt) * | 2003-12-22 | 2007-04-27 | Genzyme Corp | anticorpo anti-cd52 para tratamento da diabetes |
| CN104610422A (zh) * | 2005-03-11 | 2015-05-13 | 惠氏公司 | 弱分配层析的方法 |
| KR101463631B1 (ko) | 2006-03-31 | 2014-11-19 | 추가이 세이야쿠 가부시키가이샤 | 항체의 혈중 동태를 제어하는 방법 |
| RU2510400C9 (ru) | 2007-09-26 | 2014-07-20 | Чугаи Сейяку Кабусики Кайся | Способ модификации изоэлектрической точки антитела с помощью аминокислотных замен в cdr |
| US20110111406A1 (en) | 2008-04-11 | 2011-05-12 | Chugai Seiyaku Kabushiki Kaisha | Antigen-binding molecule capable of binding to two or more antigen molecules repeatedly |
| AU2010248935B2 (en) | 2009-05-13 | 2016-12-15 | Genzyme Corporation | Methods and compositions for treating lupus |
| SG176060A1 (en) | 2009-05-13 | 2011-12-29 | Genzyme Corp | Anti-human cd52 immunoglobulins |
| WO2011090719A2 (en) * | 2009-12-29 | 2011-07-28 | Dr. Reddy's Laboratories Ltd. | Protein purification by ion exchange |
| US20130096284A1 (en) | 2010-06-21 | 2013-04-18 | Kyowa Hakko Kirin Co., Ltd. | Method for purifying protein using amino acid |
| RU2467783C2 (ru) * | 2010-07-30 | 2012-11-27 | Закрытое акционерное общество "БиоХимМак СТ" | Способ хроматографического выделения иммуноглобулина |
| WO2012073992A1 (ja) | 2010-11-30 | 2012-06-07 | 中外製薬株式会社 | 複数分子の抗原に繰り返し結合する抗原結合分子 |
| US9062106B2 (en) | 2011-04-27 | 2015-06-23 | Abbvie Inc. | Methods for controlling the galactosylation profile of recombinantly-expressed proteins |
| GB201109238D0 (en) * | 2011-06-01 | 2011-07-13 | Antitope Ltd | Antibodies |
| US9067990B2 (en) | 2013-03-14 | 2015-06-30 | Abbvie, Inc. | Protein purification using displacement chromatography |
| WO2013158273A1 (en) | 2012-04-20 | 2013-10-24 | Abbvie Inc. | Methods to modulate c-terminal lysine variant distribution |
| US9334319B2 (en) | 2012-04-20 | 2016-05-10 | Abbvie Inc. | Low acidic species compositions |
| WO2013176754A1 (en) | 2012-05-24 | 2013-11-28 | Abbvie Inc. | Novel purification of antibodies using hydrophobic interaction chromatography |
| US9650411B2 (en) | 2012-08-07 | 2017-05-16 | Kyowa Hakko Kirin Co., Ltd. | Method of purifying protein |
| WO2014035475A1 (en) | 2012-09-02 | 2014-03-06 | Abbvie Inc. | Methods to control protein heterogeneity |
| US9512214B2 (en) | 2012-09-02 | 2016-12-06 | Abbvie, Inc. | Methods to control protein heterogeneity |
| CA2905010A1 (en) | 2013-03-12 | 2014-09-18 | Abbvie Inc. | Human antibodies that bind human tnf-alpha and methods of preparing the same |
| US8921526B2 (en) | 2013-03-14 | 2014-12-30 | Abbvie, Inc. | Mutated anti-TNFα antibodies and methods of their use |
| US9499614B2 (en) | 2013-03-14 | 2016-11-22 | Abbvie Inc. | Methods for modulating protein glycosylation profiles of recombinant protein therapeutics using monosaccharides and oligosaccharides |
| US9017687B1 (en) | 2013-10-18 | 2015-04-28 | Abbvie, Inc. | Low acidic species compositions and methods for producing and using the same using displacement chromatography |
| AU2013203043B2 (en) * | 2013-03-15 | 2016-10-06 | Takeda Pharmaceutical Company Limited | Methods to produce a human plasma-derived igg preparation enriched in brain disease-related natural iggs |
| AR095199A1 (es) | 2013-03-15 | 2015-09-30 | Genzyme Corp | Anticuerpos anti-cd52 |
| EP3052640A2 (en) | 2013-10-04 | 2016-08-10 | AbbVie Inc. | Use of metal ions for modulation of protein glycosylation profiles of recombinant proteins |
| US9181337B2 (en) | 2013-10-18 | 2015-11-10 | Abbvie, Inc. | Modulated lysine variant species compositions and methods for producing and using the same |
| US9085618B2 (en) | 2013-10-18 | 2015-07-21 | Abbvie, Inc. | Low acidic species compositions and methods for producing and using the same |
| US8946395B1 (en) | 2013-10-18 | 2015-02-03 | Abbvie Inc. | Purification of proteins using hydrophobic interaction chromatography |
| WO2015073884A2 (en) | 2013-11-15 | 2015-05-21 | Abbvie, Inc. | Glycoengineered binding protein compositions |
| BR112016014824A2 (pt) | 2013-12-27 | 2017-09-19 | Chugai Pharmaceutical Co Ltd | Método para purificar anticorpo que tem ponto isoelétrico baixo |
| AR103161A1 (es) | 2014-12-19 | 2017-04-19 | Chugai Pharmaceutical Co Ltd | Anticuerpos antimiostatina y regiones fc variantes así como métodos de uso |
| EP3330279B1 (en) | 2015-07-31 | 2022-04-06 | Chugai Seiyaku Kabushiki Kaisha | Method for purifying composition comprising antibodies with anionic polymer |
| EP3394098A4 (en) | 2015-12-25 | 2019-11-13 | Chugai Seiyaku Kabushiki Kaisha | ANTI-MYOSTATIN ANTIBODIES AND METHODS OF USE |
| CA3031028C (en) | 2016-07-25 | 2024-02-13 | Lu Wang | Affinity chromatography wash buffer |
| EP3494991A4 (en) | 2016-08-05 | 2020-07-29 | Chugai Seiyaku Kabushiki Kaisha | COMPOSITION FOR THE PROPHYLAXIS OR TREATMENT OF IL-8 RELATED DISEASES |
| US20220177518A1 (en) | 2019-03-29 | 2022-06-09 | Asahi Kasei Medical Co., Ltd. | Method for purifying protein |
| EP3954725B1 (en) | 2019-04-08 | 2024-03-06 | Asahi Kasei Medical Co., Ltd. | Polyamide medium for purifying protein-containing solution and method for producing polyamide medium |
| TW202104244A (zh) | 2019-04-10 | 2021-02-01 | 日商中外製藥股份有限公司 | Fc區域改變抗體的純化方法 |
| JPWO2022260091A1 (cg-RX-API-DMAC7.html) | 2021-06-10 | 2022-12-15 |
Family Cites Families (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5118796A (en) * | 1987-12-09 | 1992-06-02 | Centocor, Incorporated | Efficient large-scale purification of immunoglobulins and derivatives |
| DE68909441T2 (de) * | 1988-02-12 | 1994-02-10 | British Tech Group | Modifizierte Antikörper. |
-
1990
- 1990-10-17 GB GB909022547A patent/GB9022547D0/en active Pending
-
1991
- 1991-10-16 FR FR9112738A patent/FR2668164A1/fr active Granted
- 1991-10-16 IE IE356091A patent/IE913560A1/en not_active IP Right Cessation
- 1991-10-16 TW TW080108178A patent/TW283710B/zh not_active IP Right Cessation
- 1991-10-16 IT ITRM910788A patent/IT1250064B/it active IP Right Grant
- 1991-10-16 IL IL10272691A patent/IL102726A/en not_active IP Right Cessation
- 1991-10-16 GR GR910100425A patent/GR910100425A/el unknown
- 1991-10-16 BE BE9100946A patent/BE1004226A5/fr not_active IP Right Cessation
- 1991-10-16 MY MYPI91001909A patent/MY119030A/en unknown
- 1991-10-16 ZA ZA918259A patent/ZA918259B/xx unknown
- 1991-10-16 MY MYPI92001385A patent/MY136210A/en unknown
- 1991-10-16 PT PT99248A patent/PT99248B/pt not_active IP Right Cessation
- 1991-10-16 NZ NZ244114A patent/NZ244114A/en not_active IP Right Cessation
- 1991-10-16 NZ NZ240247A patent/NZ240247A/en not_active IP Right Cessation
- 1991-10-16 IL IL99761A patent/IL99761A0/xx unknown
- 1991-10-16 ZA ZA926191A patent/ZA926191B/xx unknown
- 1991-10-17 AT AT91917891T patent/ATE162552T1/de not_active IP Right Cessation
- 1991-10-17 AT AT0900791A patent/ATA900791A/de not_active Application Discontinuation
- 1991-10-17 ES ES91917891T patent/ES2112865T5/es not_active Expired - Lifetime
- 1991-10-17 EP EP91917891A patent/EP0504363B2/en not_active Expired - Lifetime
- 1991-10-17 DK DK91917891T patent/DK0504363T4/da active
- 1991-10-17 WO PCT/GB1991/001816 patent/WO1992007084A1/en not_active Ceased
- 1991-10-17 ES ES09250029A patent/ES2081742B1/es not_active Expired - Lifetime
- 1991-10-17 CA CA002069481A patent/CA2069481C/en not_active Expired - Lifetime
- 1991-10-17 KR KR1019920701427A patent/KR960015399B1/ko not_active Expired - Lifetime
- 1991-10-17 CH CH2655/92A patent/CH681455A5/fr not_active IP Right Cessation
- 1991-10-17 JP JP3516509A patent/JP2638680B2/ja not_active Expired - Lifetime
- 1991-10-17 DE DE69128774T patent/DE69128774T3/de not_active Expired - Lifetime
- 1991-10-17 CH CH1901/92A patent/CH681305A5/fr not_active IP Right Cessation
- 1991-10-17 HU HU9202000A patent/HUT64601A/hu unknown
-
1992
- 1992-02-28 GB GB9209529A patent/GB2253397A/en not_active Withdrawn
- 1992-05-25 FI FI922380A patent/FI110003B/fi not_active IP Right Cessation
- 1992-05-27 LU LU88122A patent/LU88122A1/xx unknown
- 1992-06-17 FI FI922824A patent/FI110002B/fi not_active IP Right Cessation
- 1992-06-29 MX MX9203794A patent/MX9203794A/es unknown
- 1992-08-04 IL IL102726A patent/IL102726A0/xx unknown
- 1992-08-13 FR FR9209998A patent/FR2677997A1/fr not_active Withdrawn
- 1992-09-23 AU AU25321/92A patent/AU658926B2/en not_active Expired
- 1992-10-20 GR GR920100471A patent/GR920100471A/el unknown
- 1992-10-20 PT PT100988A patent/PT100988B/pt not_active IP Right Cessation
- 1992-10-30 KR KR1019920702699A patent/KR100193314B1/ko not_active Expired - Lifetime
-
1994
- 1994-08-11 AU AU70242/94A patent/AU7024294A/en not_active Abandoned
- 1994-10-07 US US08/319,598 patent/US5644036A/en not_active Expired - Lifetime
-
1997
- 1997-04-28 BR BR1100358-8A patent/BR1100358A/pt active IP Right Grant
- 1997-11-13 AU AU45218/97A patent/AU716402B2/en not_active Expired
-
1998
- 1998-04-10 GR GR980400777T patent/GR3026588T3/el unknown
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| KR960015399B1 (ko) | 면역 글로불린의 정제방법 | |
| IE84931B1 (en) | Purified IgG Antibodies | |
| DE69130912T2 (de) | Antikörperherstellung | |
| EP1075488A1 (en) | Protein purification by ion exchange chromatography | |
| KR102578087B1 (ko) | 숙주세포 갈렉틴(galectins) 및 다른 오염물(contaminant)로부터 글리코실화 단백질을 정제하는 방법 | |
| CN116547298A (zh) | 猫抗体恒定区中的突变 | |
| AU649078C (en) | Purified CDW52-specific antibodies | |
| WO1994015950A1 (en) | Purification of immunoglobulin | |
| CN119751679A (zh) | 一种抗人cd13的抗体及其相关生产方法和应用 | |
| dos Santos | An alternative capture step for monoclonal antibodies: phenylboronate as a new multi-modal ligand |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| PA0109 | Patent application |
Patent event code: PA01091R01D Comment text: Patent Application Patent event date: 19920616 |
|
| A201 | Request for examination | ||
| AMND | Amendment | ||
| PA0201 | Request for examination |
Patent event code: PA02012R01D Patent event date: 19921030 Comment text: Request for Examination of Application Patent event code: PA02011R01I Patent event date: 19920616 Comment text: Patent Application |
|
| PG1501 | Laying open of application | ||
| E902 | Notification of reason for refusal | ||
| PE0902 | Notice of grounds for rejection |
Comment text: Notification of reason for refusal Patent event date: 19950830 Patent event code: PE09021S01D |
|
| AMND | Amendment | ||
| E601 | Decision to refuse application | ||
| PE0601 | Decision on rejection of patent |
Patent event date: 19960406 Comment text: Decision to Refuse Application Patent event code: PE06012S01D Patent event date: 19950830 Comment text: Notification of reason for refusal Patent event code: PE06011S01I |
|
| J2X1 | Appeal (before the patent court) |
Free format text: APPEAL AGAINST DECISION TO DECLINE REFUSAL |
|
| PJ2001 | Appeal |
Appeal kind category: Appeal against decision to decline refusal Decision date: 19970117 Appeal identifier: 1996201001015 Request date: 19960508 |
|
| PB0901 | Examination by re-examination before a trial |
Comment text: Request for Trial against Decision on Refusal Patent event date: 19960513 Patent event code: PB09011R01I Comment text: Amendment to Specification, etc. Patent event date: 19960130 Patent event code: PB09011R02I Comment text: Amendment to Specification, etc. Patent event date: 19921030 Patent event code: PB09011R02I |
|
| G160 | Decision to publish patent application | ||
| PG1605 | Publication of application before grant of patent |
Comment text: Decision on Publication of Application Patent event code: PG16051S01I Patent event date: 19961017 |
|
| B701 | Decision to grant | ||
| PB0701 | Decision of registration after re-examination before a trial |
Patent event date: 19970117 Comment text: Decision to Grant Registration Patent event code: PB07012S01D Patent event date: 19960920 Comment text: Transfer of Trial File for Re-examination before a Trial Patent event code: PB07011S01I |
|
| GRNT | Written decision to grant | ||
| PR0701 | Registration of establishment |
Comment text: Registration of Establishment Patent event date: 19970408 Patent event code: PR07011E01D |
|
| PR1002 | Payment of registration fee |
Payment date: 19970408 End annual number: 3 Start annual number: 1 |
|
| PR1001 | Payment of annual fee |
Payment date: 19991026 Start annual number: 4 End annual number: 4 |
|
| PR1001 | Payment of annual fee |
Payment date: 20001108 Start annual number: 5 End annual number: 5 |
|
| PR1001 | Payment of annual fee |
Payment date: 20011107 Start annual number: 6 End annual number: 6 |
|
| PR1001 | Payment of annual fee |
Payment date: 20021107 Start annual number: 7 End annual number: 7 |
|
| PR1001 | Payment of annual fee |
Payment date: 20031015 Start annual number: 8 End annual number: 8 |
|
| PR1001 | Payment of annual fee |
Payment date: 20041011 Start annual number: 9 End annual number: 9 |
|
| PR1001 | Payment of annual fee |
Payment date: 20051007 Start annual number: 10 End annual number: 10 |
|
| PR1001 | Payment of annual fee |
Payment date: 20061013 Start annual number: 11 End annual number: 11 |
|
| PR1001 | Payment of annual fee |
Payment date: 20071005 Start annual number: 12 End annual number: 12 |
|
| PR1001 | Payment of annual fee |
Payment date: 20081007 Start annual number: 13 End annual number: 13 |
|
| PR1001 | Payment of annual fee |
Payment date: 20091012 Start annual number: 14 End annual number: 14 |
|
| FPAY | Annual fee payment |
Payment date: 20101029 Year of fee payment: 15 |
|
| PR1001 | Payment of annual fee |
Payment date: 20101029 Start annual number: 15 End annual number: 15 |
|
| EXPY | Expiration of term | ||
| PC1801 | Expiration of term |