JP2005508892A - Ｇｃ−グロブリンの大規模生産のための精製方法、これにより得られる物質およびそれらの医薬用途 - Google Patents
Ｇｃ−グロブリンの大規模生産のための精製方法、これにより得られる物質およびそれらの医薬用途 Download PDFInfo
- Publication number
- JP2005508892A JP2005508892A JP2003521270A JP2003521270A JP2005508892A JP 2005508892 A JP2005508892 A JP 2005508892A JP 2003521270 A JP2003521270 A JP 2003521270A JP 2003521270 A JP2003521270 A JP 2003521270A JP 2005508892 A JP2005508892 A JP 2005508892A
- Authority
- JP
- Japan
- Prior art keywords
- globulin
- exchange chromatography
- ultrafiltration
- anion exchange
- virus
- 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.)
- Withdrawn
Links
- 102000050760 Vitamin D-binding protein Human genes 0.000 title claims abstract description 292
- 101710179590 Vitamin D-binding protein Proteins 0.000 title claims abstract description 291
- 238000000034 method Methods 0.000 title claims abstract description 83
- 238000000746 purification Methods 0.000 title claims abstract description 36
- 238000011031 large-scale manufacturing process Methods 0.000 title abstract description 7
- 239000000126 substance Substances 0.000 title description 3
- 239000000243 solution Substances 0.000 claims abstract description 71
- 241000700605 Viruses Species 0.000 claims abstract description 57
- 238000004255 ion exchange chromatography Methods 0.000 claims abstract description 13
- 239000003814 drug Substances 0.000 claims abstract description 12
- 239000000725 suspension Substances 0.000 claims abstract description 11
- 238000004519 manufacturing process Methods 0.000 claims abstract description 9
- 210000004369 blood Anatomy 0.000 claims abstract description 7
- 239000008280 blood Substances 0.000 claims abstract description 7
- 230000002147 killing effect Effects 0.000 claims abstract description 7
- 235000021277 colostrum Nutrition 0.000 claims abstract description 5
- 210000003022 colostrum Anatomy 0.000 claims abstract description 5
- 235000013365 dairy product Nutrition 0.000 claims abstract description 4
- 239000006228 supernatant Substances 0.000 claims abstract description 4
- 238000002405 diagnostic procedure Methods 0.000 claims abstract description 3
- 238000000108 ultra-filtration Methods 0.000 claims description 34
- 238000011026 diafiltration Methods 0.000 claims description 31
- 239000000203 mixture Substances 0.000 claims description 31
- 102000007469 Actins Human genes 0.000 claims description 27
- 108010085238 Actins Proteins 0.000 claims description 27
- 239000000047 product Substances 0.000 claims description 27
- 238000005571 anion exchange chromatography Methods 0.000 claims description 23
- 238000009472 formulation Methods 0.000 claims description 20
- 239000003599 detergent Substances 0.000 claims description 17
- 230000008569 process Effects 0.000 claims description 16
- 239000000463 material Substances 0.000 claims description 14
- 238000005277 cation exchange chromatography Methods 0.000 claims description 13
- 238000001914 filtration Methods 0.000 claims description 13
- 239000002904 solvent Substances 0.000 claims description 13
- 239000007858 starting material Substances 0.000 claims description 13
- 238000011282 treatment Methods 0.000 claims description 13
- 238000001542 size-exclusion chromatography Methods 0.000 claims description 12
- 240000008042 Zea mays Species 0.000 claims description 11
- 235000005824 Zea mays ssp. parviglumis Nutrition 0.000 claims description 11
- 235000002017 Zea mays subsp mays Nutrition 0.000 claims description 11
- 235000005822 corn Nutrition 0.000 claims description 11
- 210000002966 serum Anatomy 0.000 claims description 11
- 238000000760 immunoelectrophoresis Methods 0.000 claims description 7
- 108010058237 plasma protein fraction Proteins 0.000 claims description 7
- 229940081857 plasma protein fraction Drugs 0.000 claims description 7
- 230000003253 viricidal effect Effects 0.000 claims description 6
- 238000011210 chromatographic step Methods 0.000 claims description 5
- 201000010099 disease Diseases 0.000 claims description 5
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 claims description 5
- 238000001728 nano-filtration Methods 0.000 claims description 5
- 206010012335 Dependence Diseases 0.000 claims description 4
- 230000009467 reduction Effects 0.000 claims description 4
- 206010028980 Neoplasm Diseases 0.000 claims description 3
- 230000007812 deficiency Effects 0.000 claims description 3
- 238000010255 intramuscular injection Methods 0.000 claims description 3
- 239000007927 intramuscular injection Substances 0.000 claims description 3
- 238000010253 intravenous injection Methods 0.000 claims description 3
- 238000010254 subcutaneous injection Methods 0.000 claims description 3
- 239000007929 subcutaneous injection Substances 0.000 claims description 3
- 206010010356 Congenital anomaly Diseases 0.000 claims description 2
- 201000011510 cancer Diseases 0.000 claims description 2
- 229940079593 drug Drugs 0.000 claims description 2
- 241000057000 ECM virus Species 0.000 claims 2
- 102000004190 Enzymes Human genes 0.000 claims 1
- 108090000790 Enzymes Proteins 0.000 claims 1
- 206010047626 Vitamin D Deficiency Diseases 0.000 claims 1
- 230000003042 antagnostic effect Effects 0.000 claims 1
- 238000003018 immunoassay Methods 0.000 claims 1
- 208000012237 paracetamol poisoning Diseases 0.000 claims 1
- 230000002265 prevention Effects 0.000 claims 1
- 230000003612 virological effect Effects 0.000 claims 1
- 230000008901 benefit Effects 0.000 abstract description 7
- 208000024172 Cardiovascular disease Diseases 0.000 abstract description 3
- 238000000855 fermentation Methods 0.000 abstract description 2
- 230000004151 fermentation Effects 0.000 abstract description 2
- 235000003869 genetically modified organism Nutrition 0.000 abstract description 2
- 239000000872 buffer Substances 0.000 description 57
- 235000018102 proteins Nutrition 0.000 description 37
- 108090000623 proteins and genes Proteins 0.000 description 37
- 102000004169 proteins and genes Human genes 0.000 description 37
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 34
- 239000011347 resin Substances 0.000 description 23
- 229920005989 resin Polymers 0.000 description 23
- 238000010828 elution Methods 0.000 description 21
- 239000012528 membrane Substances 0.000 description 19
- 229920002684 Sepharose Polymers 0.000 description 17
- 239000003957 anion exchange resin Substances 0.000 description 17
- 239000011780 sodium chloride Substances 0.000 description 17
- 239000003795 chemical substances by application Substances 0.000 description 16
- 238000005342 ion exchange Methods 0.000 description 16
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical group OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 16
- 230000027455 binding Effects 0.000 description 15
- 239000000356 contaminant Substances 0.000 description 15
- NWUYHJFMYQTDRP-UHFFFAOYSA-N 1,2-bis(ethenyl)benzene;1-ethenyl-2-ethylbenzene;styrene Chemical compound C=CC1=CC=CC=C1.CCC1=CC=CC=C1C=C.C=CC1=CC=CC=C1C=C NWUYHJFMYQTDRP-UHFFFAOYSA-N 0.000 description 14
- 230000002779 inactivation Effects 0.000 description 13
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 12
- 239000007983 Tris buffer Substances 0.000 description 12
- 238000004587 chromatography analysis Methods 0.000 description 12
- 125000002057 carboxymethyl group Chemical group [H]OC(=O)C([H])([H])[*] 0.000 description 11
- 238000005341 cation exchange Methods 0.000 description 11
- 239000011159 matrix material Substances 0.000 description 11
- 239000001488 sodium phosphate Substances 0.000 description 11
- 229910000162 sodium phosphate Inorganic materials 0.000 description 11
- 235000011008 sodium phosphates Nutrition 0.000 description 11
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 11
- MZVQCMJNVPIDEA-UHFFFAOYSA-N [CH2]CN(CC)CC Chemical compound [CH2]CN(CC)CC MZVQCMJNVPIDEA-UHFFFAOYSA-N 0.000 description 10
- 239000003729 cation exchange resin Substances 0.000 description 10
- 238000005349 anion exchange Methods 0.000 description 9
- 230000000415 inactivating effect Effects 0.000 description 9
- 150000003839 salts Chemical class 0.000 description 9
- 229930003316 Vitamin D Natural products 0.000 description 8
- QYSXJUFSXHHAJI-XFEUOLMDSA-N Vitamin D3 Natural products C1(/[C@@H]2CC[C@@H]([C@]2(CCC1)C)[C@H](C)CCCC(C)C)=C/C=C1\C[C@@H](O)CCC1=C QYSXJUFSXHHAJI-XFEUOLMDSA-N 0.000 description 8
- 239000006167 equilibration buffer Substances 0.000 description 8
- 235000019166 vitamin D Nutrition 0.000 description 8
- 239000011710 vitamin D Substances 0.000 description 8
- 150000003710 vitamin D derivatives Chemical class 0.000 description 8
- 229940046008 vitamin d Drugs 0.000 description 8
- 230000000694 effects Effects 0.000 description 7
- 208000015181 infectious disease Diseases 0.000 description 7
- 230000002458 infectious effect Effects 0.000 description 7
- 150000002632 lipids Chemical class 0.000 description 7
- 239000002245 particle Substances 0.000 description 7
- 238000011084 recovery Methods 0.000 description 7
- 238000005406 washing Methods 0.000 description 7
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 6
- 108060003951 Immunoglobulin Proteins 0.000 description 6
- 238000004458 analytical method Methods 0.000 description 6
- 238000001962 electrophoresis Methods 0.000 description 6
- 238000011067 equilibration Methods 0.000 description 6
- 102000018358 immunoglobulin Human genes 0.000 description 6
- 235000010482 polyoxyethylene sorbitan monooleate Nutrition 0.000 description 6
- 229920000053 polysorbate 80 Polymers 0.000 description 6
- RZVAJINKPMORJF-UHFFFAOYSA-N Acetaminophen Chemical compound CC(=O)NC1=CC=C(O)C=C1 RZVAJINKPMORJF-UHFFFAOYSA-N 0.000 description 5
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 5
- 238000004113 cell culture Methods 0.000 description 5
- 229910052588 hydroxylapatite Inorganic materials 0.000 description 5
- XYJRXVWERLGGKC-UHFFFAOYSA-D pentacalcium;hydroxide;triphosphate Chemical compound [OH-].[Ca+2].[Ca+2].[Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O XYJRXVWERLGGKC-UHFFFAOYSA-D 0.000 description 5
- 239000002953 phosphate buffered saline Substances 0.000 description 5
- 229920002492 poly(sulfone) Polymers 0.000 description 5
- GUBGYTABKSRVRQ-WFVLMXAXSA-N DEAE-cellulose Chemical compound OC1C(O)C(O)C(CO)O[C@H]1O[C@@H]1C(CO)OC(O)C(O)C1O GUBGYTABKSRVRQ-WFVLMXAXSA-N 0.000 description 4
- 102000002151 Microfilament Proteins Human genes 0.000 description 4
- 108010040897 Microfilament Proteins Proteins 0.000 description 4
- 239000012564 Q sepharose fast flow resin Substances 0.000 description 4
- 229920005654 Sephadex Polymers 0.000 description 4
- 238000010266 Sephadex chromatography Methods 0.000 description 4
- 239000012507 Sephadex™ Substances 0.000 description 4
- 239000011543 agarose gel Substances 0.000 description 4
- 150000001450 anions Chemical class 0.000 description 4
- 239000001913 cellulose Substances 0.000 description 4
- 229920002678 cellulose Polymers 0.000 description 4
- 238000000605 extraction Methods 0.000 description 4
- 238000011534 incubation Methods 0.000 description 4
- 208000014674 injury Diseases 0.000 description 4
- 239000003456 ion exchange resin Substances 0.000 description 4
- 229920003303 ion-exchange polymer Polymers 0.000 description 4
- 239000012669 liquid formulation Substances 0.000 description 4
- 210000004185 liver Anatomy 0.000 description 4
- 229960005489 paracetamol Drugs 0.000 description 4
- 239000008363 phosphate buffer Substances 0.000 description 4
- 238000011002 quantification Methods 0.000 description 4
- 230000035939 shock Effects 0.000 description 4
- 239000007790 solid phase Substances 0.000 description 4
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 3
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 3
- 108010017384 Blood Proteins Proteins 0.000 description 3
- 102000004506 Blood Proteins Human genes 0.000 description 3
- 102000006395 Globulins Human genes 0.000 description 3
- 108010044091 Globulins Proteins 0.000 description 3
- 101000956004 Homo sapiens Vitamin D-binding protein Proteins 0.000 description 3
- 241000700159 Rattus Species 0.000 description 3
- 238000012870 ammonium sulfate precipitation Methods 0.000 description 3
- 239000007853 buffer solution Substances 0.000 description 3
- 238000005119 centrifugation Methods 0.000 description 3
- 230000008859 change Effects 0.000 description 3
- 230000003247 decreasing effect Effects 0.000 description 3
- 238000000502 dialysis Methods 0.000 description 3
- 238000010790 dilution Methods 0.000 description 3
- 239000012895 dilution Substances 0.000 description 3
- 230000005714 functional activity Effects 0.000 description 3
- 239000012133 immunoprecipitate Substances 0.000 description 3
- 230000000937 inactivator Effects 0.000 description 3
- 238000002372 labelling Methods 0.000 description 3
- 210000002540 macrophage Anatomy 0.000 description 3
- 230000003204 osmotic effect Effects 0.000 description 3
- 229920001223 polyethylene glycol Polymers 0.000 description 3
- 238000002360 preparation method Methods 0.000 description 3
- 239000012064 sodium phosphate buffer Substances 0.000 description 3
- 239000003381 stabilizer Substances 0.000 description 3
- -1 sulfopropyl Chemical group 0.000 description 3
- 230000008733 trauma Effects 0.000 description 3
- 239000011534 wash buffer Substances 0.000 description 3
- OWEGMIWEEQEYGQ-UHFFFAOYSA-N 100676-05-9 Natural products OC1C(O)C(O)C(CO)OC1OCC1C(O)C(O)C(O)C(OC2C(OC(O)C(O)C2O)CO)O1 OWEGMIWEEQEYGQ-UHFFFAOYSA-N 0.000 description 2
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 2
- 125000000022 2-aminoethyl group Chemical group [H]C([*])([H])C([H])([H])N([H])[H] 0.000 description 2
- XZKIHKMTEMTJQX-UHFFFAOYSA-N 4-Nitrophenyl Phosphate Chemical compound OP(O)(=O)OC1=CC=C([N+]([O-])=O)C=C1 XZKIHKMTEMTJQX-UHFFFAOYSA-N 0.000 description 2
- 229920000936 Agarose Polymers 0.000 description 2
- 108010088751 Albumins Proteins 0.000 description 2
- 102000009027 Albumins Human genes 0.000 description 2
- 241000283707 Capra Species 0.000 description 2
- WQZGKKKJIJFFOK-QTVWNMPRSA-N D-mannopyranose Chemical compound OC[C@H]1OC(O)[C@@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-QTVWNMPRSA-N 0.000 description 2
- 229920002307 Dextran Polymers 0.000 description 2
- 238000002965 ELISA Methods 0.000 description 2
- 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 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- 241000424725 Heide Species 0.000 description 2
- GUBGYTABKSRVRQ-PICCSMPSSA-N Maltose Natural products O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@@H](CO)OC(O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-PICCSMPSSA-N 0.000 description 2
- 241000124008 Mammalia Species 0.000 description 2
- 241000283973 Oryctolagus cuniculus Species 0.000 description 2
- 239000002202 Polyethylene glycol Substances 0.000 description 2
- 229920001213 Polysorbate 20 Polymers 0.000 description 2
- 229920002472 Starch Polymers 0.000 description 2
- 241000701093 Suid alphaherpesvirus 1 Species 0.000 description 2
- 230000003213 activating effect Effects 0.000 description 2
- 238000001042 affinity chromatography Methods 0.000 description 2
- 239000007900 aqueous suspension Substances 0.000 description 2
- 239000000022 bacteriostatic agent Substances 0.000 description 2
- 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 2
- GUBGYTABKSRVRQ-QUYVBRFLSA-N beta-maltose Chemical compound OC[C@H]1O[C@H](O[C@H]2[C@H](O)[C@@H](O)[C@H](O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@@H]1O GUBGYTABKSRVRQ-QUYVBRFLSA-N 0.000 description 2
- 230000015572 biosynthetic process Effects 0.000 description 2
- 230000037396 body weight Effects 0.000 description 2
- 239000006285 cell suspension Substances 0.000 description 2
- 238000004440 column chromatography Methods 0.000 description 2
- 230000002860 competitive effect Effects 0.000 description 2
- 239000012141 concentrate Substances 0.000 description 2
- NKLPQNGYXWVELD-UHFFFAOYSA-M coomassie brilliant blue Chemical compound [Na+].C1=CC(OCC)=CC=C1NC1=CC=C(C(=C2C=CC(C=C2)=[N+](CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=2C=CC(=CC=2)N(CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=C1 NKLPQNGYXWVELD-UHFFFAOYSA-M 0.000 description 2
- 230000006378 damage Effects 0.000 description 2
- 230000002950 deficient Effects 0.000 description 2
- 230000015961 delipidation Effects 0.000 description 2
- 239000013578 denaturing buffer Substances 0.000 description 2
- 229940042399 direct acting antivirals protease inhibitors Drugs 0.000 description 2
- 239000012149 elution buffer Substances 0.000 description 2
- 238000011049 filling Methods 0.000 description 2
- 239000013020 final formulation Substances 0.000 description 2
- 239000012467 final product Substances 0.000 description 2
- 238000001502 gel electrophoresis Methods 0.000 description 2
- 239000008103 glucose Substances 0.000 description 2
- 206010019692 hepatic necrosis Diseases 0.000 description 2
- 238000004128 high performance liquid chromatography Methods 0.000 description 2
- 229940072221 immunoglobulins Drugs 0.000 description 2
- 238000001802 infusion Methods 0.000 description 2
- 238000001990 intravenous administration Methods 0.000 description 2
- 150000002500 ions Chemical class 0.000 description 2
- 239000000644 isotonic solution Substances 0.000 description 2
- 229910000403 monosodium phosphate Inorganic materials 0.000 description 2
- 235000019799 monosodium phosphate Nutrition 0.000 description 2
- 244000309711 non-enveloped viruses Species 0.000 description 2
- WWZKQHOCKIZLMA-UHFFFAOYSA-N octanoic acid Chemical compound CCCCCCCC(O)=O WWZKQHOCKIZLMA-UHFFFAOYSA-N 0.000 description 2
- 239000000137 peptide hydrolase inhibitor Substances 0.000 description 2
- 239000000825 pharmaceutical preparation Substances 0.000 description 2
- 229940127557 pharmaceutical product Drugs 0.000 description 2
- YBYRMVIVWMBXKQ-UHFFFAOYSA-N phenylmethanesulfonyl fluoride Chemical compound FS(=O)(=O)CC1=CC=CC=C1 YBYRMVIVWMBXKQ-UHFFFAOYSA-N 0.000 description 2
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 2
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 2
- 239000011148 porous material Substances 0.000 description 2
- 238000012545 processing Methods 0.000 description 2
- 238000001742 protein purification Methods 0.000 description 2
- 229940124272 protein stabilizer Drugs 0.000 description 2
- 125000001453 quaternary ammonium group Chemical group 0.000 description 2
- 238000011946 reduction process Methods 0.000 description 2
- 230000002829 reductive effect Effects 0.000 description 2
- 238000000926 separation method Methods 0.000 description 2
- 239000000377 silicon dioxide Substances 0.000 description 2
- AJPJDKMHJJGVTQ-UHFFFAOYSA-M sodium dihydrogen phosphate Chemical compound [Na+].OP(O)([O-])=O AJPJDKMHJJGVTQ-UHFFFAOYSA-M 0.000 description 2
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 2
- 238000001179 sorption measurement Methods 0.000 description 2
- 238000010186 staining Methods 0.000 description 2
- 239000008107 starch Substances 0.000 description 2
- 235000019698 starch Nutrition 0.000 description 2
- 235000000346 sugar Nutrition 0.000 description 2
- 150000008163 sugars Chemical class 0.000 description 2
- 230000001225 therapeutic effect Effects 0.000 description 2
- 238000000539 two dimensional gel electrophoresis Methods 0.000 description 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
- HDTRYLNUVZCQOY-UHFFFAOYSA-N α-D-glucopyranosyl-α-D-glucopyranoside Natural products OC1C(O)C(O)C(CO)OC1OC1C(O)C(O)C(O)C(CO)O1 HDTRYLNUVZCQOY-UHFFFAOYSA-N 0.000 description 1
- JYEUMXHLPRZUAT-UHFFFAOYSA-N 1,2,3-triazine Chemical compound C1=CN=NN=C1 JYEUMXHLPRZUAT-UHFFFAOYSA-N 0.000 description 1
- HSGVYKDZIBXVOY-UHFFFAOYSA-N 1,3-diazinane-2,4,6-trione 2-hydroxypropanoic acid Chemical compound CC(O)C(O)=O.O=C1CC(=O)NC(=O)N1.O=C1CC(=O)NC(=O)N1.O=C1CC(=O)NC(=O)N1 HSGVYKDZIBXVOY-UHFFFAOYSA-N 0.000 description 1
- CFBILACNYSPRPM-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;2-[[1,3-dihydroxy-2-(hydroxymethyl)propan-2-yl]amino]acetic acid Chemical compound OCC(N)(CO)CO.OCC(CO)(CO)NCC(O)=O CFBILACNYSPRPM-UHFFFAOYSA-N 0.000 description 1
- HRPVXLWXLXDGHG-UHFFFAOYSA-N Acrylamide Chemical compound NC(=O)C=C HRPVXLWXLXDGHG-UHFFFAOYSA-N 0.000 description 1
- PAYRUJLWNCNPSJ-UHFFFAOYSA-N Aniline Chemical compound NC1=CC=CC=C1 PAYRUJLWNCNPSJ-UHFFFAOYSA-N 0.000 description 1
- 101710081722 Antitrypsin Proteins 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 206010006187 Breast cancer Diseases 0.000 description 1
- 208000026310 Breast neoplasm Diseases 0.000 description 1
- 238000002238 CM-cellulose chromatography Methods 0.000 description 1
- 239000005635 Caprylic acid (CAS 124-07-2) Substances 0.000 description 1
- 206010053567 Coagulopathies Diseases 0.000 description 1
- 108010032608 Cohn fraction IV Proteins 0.000 description 1
- 206010009944 Colon cancer Diseases 0.000 description 1
- 241000724252 Cucumber mosaic virus Species 0.000 description 1
- FBPFZTCFMRRESA-FSIIMWSLSA-N D-Glucitol Natural products OC[C@H](O)[C@H](O)[C@@H](O)[C@H](O)CO FBPFZTCFMRRESA-FSIIMWSLSA-N 0.000 description 1
- FBPFZTCFMRRESA-JGWLITMVSA-N D-glucitol Chemical compound OC[C@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-JGWLITMVSA-N 0.000 description 1
- 229920002271 DEAE-Sepharose Polymers 0.000 description 1
- 102100021238 Dynamin-2 Human genes 0.000 description 1
- 238000012286 ELISA Assay Methods 0.000 description 1
- 206010016654 Fibrosis Diseases 0.000 description 1
- 102000004878 Gelsolin Human genes 0.000 description 1
- 108090001064 Gelsolin Proteins 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- HTTJABKRGRZYRN-UHFFFAOYSA-N Heparin Chemical compound OC1C(NC(=O)C)C(O)OC(COS(O)(=O)=O)C1OC1C(OS(O)(=O)=O)C(O)C(OC2C(C(OS(O)(=O)=O)C(OC3C(C(O)C(O)C(O3)C(O)=O)OS(O)(=O)=O)C(CO)O2)NS(O)(=O)=O)C(C(O)=O)O1 HTTJABKRGRZYRN-UHFFFAOYSA-N 0.000 description 1
- 241000709721 Hepatovirus A Species 0.000 description 1
- 101000817607 Homo sapiens Dynamin-2 Proteins 0.000 description 1
- 241000701044 Human gammaherpesvirus 4 Species 0.000 description 1
- 241000713772 Human immunodeficiency virus 1 Species 0.000 description 1
- 241000713340 Human immunodeficiency virus 2 Species 0.000 description 1
- 241000702617 Human parvovirus B19 Species 0.000 description 1
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 1
- 208000007924 IgA Deficiency Diseases 0.000 description 1
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
- 206010061218 Inflammation Diseases 0.000 description 1
- 206010058467 Lung neoplasm malignant Diseases 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
- 208000001940 Massive Hepatic Necrosis Diseases 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- AFVFQIVMOAPDHO-UHFFFAOYSA-M Methanesulfonate Chemical compound CS([O-])(=O)=O AFVFQIVMOAPDHO-UHFFFAOYSA-M 0.000 description 1
- 208000004221 Multiple Trauma Diseases 0.000 description 1
- 102000005348 Neuraminidase Human genes 0.000 description 1
- 108010006232 Neuraminidase Proteins 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-L Phosphate ion(2-) Chemical compound OP([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-L 0.000 description 1
- 208000005374 Poisoning Diseases 0.000 description 1
- 102000029797 Prion Human genes 0.000 description 1
- 108091000054 Prion Proteins 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 1
- 206010039203 Road traffic accident Diseases 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- 206010039915 Selective IgA immunodeficiency Diseases 0.000 description 1
- 206010040070 Septic Shock Diseases 0.000 description 1
- 208000000453 Skin Neoplasms Diseases 0.000 description 1
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 1
- 208000005718 Stomach Neoplasms Diseases 0.000 description 1
- 229930006000 Sucrose Natural products 0.000 description 1
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 1
- QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 description 1
- 239000012505 Superdex™ Substances 0.000 description 1
- 208000007536 Thrombosis Diseases 0.000 description 1
- HDTRYLNUVZCQOY-WSWWMNSNSA-N Trehalose Natural products O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@H](O)[C@@H](O)[C@@H](O)[C@@H](CO)O1 HDTRYLNUVZCQOY-WSWWMNSNSA-N 0.000 description 1
- 239000007997 Tricine buffer Substances 0.000 description 1
- 239000013504 Triton X-100 Substances 0.000 description 1
- 229920004890 Triton X-100 Polymers 0.000 description 1
- 108700021020 Vitamin D-binding protein Proteins 0.000 description 1
- 208000027418 Wounds and injury Diseases 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 238000003916 acid precipitation Methods 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 239000002671 adjuvant Substances 0.000 description 1
- HDTRYLNUVZCQOY-LIZSDCNHSA-N alpha,alpha-trehalose Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 HDTRYLNUVZCQOY-LIZSDCNHSA-N 0.000 description 1
- 150000001413 amino acids Chemical class 0.000 description 1
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 1
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 1
- 235000011130 ammonium sulphate Nutrition 0.000 description 1
- 208000003455 anaphylaxis Diseases 0.000 description 1
- 238000010171 animal model Methods 0.000 description 1
- 230000001475 anti-trypsic effect Effects 0.000 description 1
- 230000000259 anti-tumor effect Effects 0.000 description 1
- 239000004019 antithrombin Substances 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- 150000001540 azides Chemical class 0.000 description 1
- 102000005936 beta-Galactosidase Human genes 0.000 description 1
- 108010005774 beta-Galactosidase Proteins 0.000 description 1
- 230000000903 blocking effect Effects 0.000 description 1
- 239000010836 blood and blood product Substances 0.000 description 1
- 230000017531 blood circulation Effects 0.000 description 1
- 229940125691 blood product Drugs 0.000 description 1
- 238000005251 capillar electrophoresis Methods 0.000 description 1
- 239000002775 capsule Substances 0.000 description 1
- 125000002091 cationic group Chemical group 0.000 description 1
- 150000001768 cations Chemical class 0.000 description 1
- 210000004027 cell Anatomy 0.000 description 1
- 230000005779 cell damage Effects 0.000 description 1
- 208000037887 cell injury Diseases 0.000 description 1
- 229910010293 ceramic material Inorganic materials 0.000 description 1
- 150000005829 chemical entities Chemical class 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- YKCWQPZFAFZLBI-UHFFFAOYSA-N cibacron blue Chemical compound C1=2C(=O)C3=CC=CC=C3C(=O)C=2C(N)=C(S(O)(=O)=O)C=C1NC(C=C1S(O)(=O)=O)=CC=C1NC(N=1)=NC(Cl)=NC=1NC1=CC=CC=C1S(O)(=O)=O YKCWQPZFAFZLBI-UHFFFAOYSA-N 0.000 description 1
- 230000007882 cirrhosis Effects 0.000 description 1
- 208000019425 cirrhosis of liver Diseases 0.000 description 1
- 230000007012 clinical effect Effects 0.000 description 1
- 230000035602 clotting Effects 0.000 description 1
- 208000029742 colonic neoplasm Diseases 0.000 description 1
- 238000004040 coloring Methods 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 239000000470 constituent Substances 0.000 description 1
- 238000011109 contamination Methods 0.000 description 1
- 239000012228 culture supernatant Substances 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 150000002016 disaccharides Chemical class 0.000 description 1
- 238000011038 discontinuous diafiltration by volume reduction Methods 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
- 238000002086 displacement chromatography Methods 0.000 description 1
- 208000009190 disseminated intravascular coagulation Diseases 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- 239000000975 dye Substances 0.000 description 1
- 230000004064 dysfunction Effects 0.000 description 1
- 230000002526 effect on cardiovascular system Effects 0.000 description 1
- 238000007823 electrophoretic assay Methods 0.000 description 1
- 238000002337 electrophoretic mobility shift assay Methods 0.000 description 1
- 238000012869 ethanol precipitation Methods 0.000 description 1
- 239000002031 ethanolic fraction Substances 0.000 description 1
- 230000007717 exclusion Effects 0.000 description 1
- 239000000284 extract Substances 0.000 description 1
- 239000011536 extraction buffer Substances 0.000 description 1
- 239000000706 filtrate Substances 0.000 description 1
- 238000005194 fractionation Methods 0.000 description 1
- 206010017758 gastric cancer Diseases 0.000 description 1
- 239000000499 gel Substances 0.000 description 1
- 238000001641 gel filtration chromatography Methods 0.000 description 1
- 238000011553 hamster model Methods 0.000 description 1
- 230000009931 harmful effect Effects 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 229960002897 heparin Drugs 0.000 description 1
- 229920000669 heparin Polymers 0.000 description 1
- 230000007866 hepatic necrosis Effects 0.000 description 1
- 208000006454 hepatitis Diseases 0.000 description 1
- 231100000283 hepatitis Toxicity 0.000 description 1
- 229910000041 hydrogen chloride Inorganic materials 0.000 description 1
- IXCSERBJSXMMFS-UHFFFAOYSA-N hydrogen chloride Substances Cl.Cl IXCSERBJSXMMFS-UHFFFAOYSA-N 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 238000004191 hydrophobic interaction chromatography Methods 0.000 description 1
- 201000007156 immunoglobulin alpha deficiency Diseases 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 239000012535 impurity Substances 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 230000004968 inflammatory condition Effects 0.000 description 1
- 230000004054 inflammatory process Effects 0.000 description 1
- 238000002347 injection Methods 0.000 description 1
- 239000007924 injection Substances 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 238000001155 isoelectric focusing Methods 0.000 description 1
- FZWBNHMXJMCXLU-BLAUPYHCSA-N isomaltotriose Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1OC[C@@H]1[C@@H](O)[C@H](O)[C@@H](O)[C@@H](OC[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C=O)O1 FZWBNHMXJMCXLU-BLAUPYHCSA-N 0.000 description 1
- 210000003734 kidney Anatomy 0.000 description 1
- 239000003446 ligand Substances 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 239000007791 liquid phase Substances 0.000 description 1
- 239000012263 liquid product Substances 0.000 description 1
- 231100000149 liver necrosis Toxicity 0.000 description 1
- 238000011068 loading method Methods 0.000 description 1
- 201000005202 lung cancer Diseases 0.000 description 1
- 208000020816 lung neoplasm Diseases 0.000 description 1
- 210000004962 mammalian cell Anatomy 0.000 description 1
- 238000004949 mass spectrometry Methods 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 208000030159 metabolic disease Diseases 0.000 description 1
- CXKWCBBOMKCUKX-UHFFFAOYSA-M methylene blue Chemical compound [Cl-].C1=CC(N(C)C)=CC2=[S+]C3=CC(N(C)C)=CC=C3N=C21 CXKWCBBOMKCUKX-UHFFFAOYSA-M 0.000 description 1
- 229960000907 methylthioninium chloride Drugs 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 235000013336 milk Nutrition 0.000 description 1
- 239000008267 milk Substances 0.000 description 1
- 210000004080 milk Anatomy 0.000 description 1
- 150000002772 monosaccharides Chemical class 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- 229960002446 octanoic acid Drugs 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 235000021317 phosphate Nutrition 0.000 description 1
- 150000003013 phosphoric acid derivatives Chemical class 0.000 description 1
- 230000036470 plasma concentration Effects 0.000 description 1
- 231100000572 poisoning Toxicity 0.000 description 1
- 230000000607 poisoning effect Effects 0.000 description 1
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
- 239000002244 precipitate Substances 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 238000002203 pretreatment Methods 0.000 description 1
- 235000004252 protein component Nutrition 0.000 description 1
- 239000012460 protein solution Substances 0.000 description 1
- 230000017854 proteolysis Effects 0.000 description 1
- 238000004445 quantitative analysis Methods 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 239000013049 sediment Substances 0.000 description 1
- 208000029138 selective IgA deficiency disease Diseases 0.000 description 1
- 230000036303 septic shock Effects 0.000 description 1
- 238000003998 size exclusion chromatography high performance liquid chromatography Methods 0.000 description 1
- 201000000849 skin cancer Diseases 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- 235000017281 sodium acetate Nutrition 0.000 description 1
- 239000001632 sodium acetate Substances 0.000 description 1
- 239000011877 solvent mixture Substances 0.000 description 1
- 239000000600 sorbitol Substances 0.000 description 1
- 239000003270 steroid hormone Substances 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 201000011549 stomach cancer Diseases 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 239000005720 sucrose Substances 0.000 description 1
- 150000005846 sugar alcohols Chemical class 0.000 description 1
- 125000000472 sulfonyl group Chemical group *S(*)(=O)=O 0.000 description 1
- 230000004083 survival effect Effects 0.000 description 1
- 208000011580 syndromic disease Diseases 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 229920001059 synthetic polymer Polymers 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- RTKIYNMVFMVABJ-UHFFFAOYSA-L thimerosal Chemical compound [Na+].CC[Hg]SC1=CC=CC=C1C([O-])=O RTKIYNMVFMVABJ-UHFFFAOYSA-L 0.000 description 1
- 230000000451 tissue damage Effects 0.000 description 1
- 231100000827 tissue damage Toxicity 0.000 description 1
- 230000009261 transgenic effect Effects 0.000 description 1
- STCOOQWBFONSKY-UHFFFAOYSA-N tributyl phosphate Chemical group CCCCOP(=O)(OCCCC)OCCCC STCOOQWBFONSKY-UHFFFAOYSA-N 0.000 description 1
- 239000002753 trypsin inhibitor Substances 0.000 description 1
- 238000013060 ultrafiltration and diafiltration Methods 0.000 description 1
- 238000009281 ultraviolet germicidal irradiation Methods 0.000 description 1
- 241001529453 unidentified herpesvirus Species 0.000 description 1
- 238000010200 validation analysis Methods 0.000 description 1
- 239000013621 viresolve pro solution Substances 0.000 description 1
- 210000005253 yeast cell Anatomy 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- A61K38/1703—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- A61K38/1709—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P3/00—Drugs for disorders of the metabolism
- A61P3/02—Nutrients, e.g. vitamins, minerals
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P39/00—General protective or antinoxious agents
- A61P39/02—Antidotes
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P7/00—Drugs for disorders of the blood or the extracellular fluid
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Animal Behavior & Ethology (AREA)
- Pharmacology & Pharmacy (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Zoology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Toxicology (AREA)
- Diabetes (AREA)
- Gastroenterology & Hepatology (AREA)
- Hematology (AREA)
- Immunology (AREA)
- Nutrition Science (AREA)
- Molecular Biology (AREA)
- Biophysics (AREA)
- Marine Sciences & Fisheries (AREA)
- Biochemistry (AREA)
- Epidemiology (AREA)
- Genetics & Genomics (AREA)
- Obesity (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Peptides Or Proteins (AREA)
- Apparatus For Disinfection Or Sterilisation (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Separation Using Semi-Permeable Membranes (AREA)
- Treatment Of Liquids With Adsorbents In General (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| DKPA200101217 | 2001-08-14 | ||
| PCT/DK2002/000531 WO2003016348A2 (en) | 2001-08-14 | 2002-08-12 | A purification process for large scale production of gc-globulin, product obtained thereby and their use in medicine |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JP2005508892A true JP2005508892A (ja) | 2005-04-07 |
| JP2005508892A5 JP2005508892A5 (enExample) | 2006-01-05 |
Family
ID=8160667
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2003521270A Withdrawn JP2005508892A (ja) | 2001-08-14 | 2002-08-12 | Ｇｃ−グロブリンの大規模生産のための精製方法、これにより得られる物質およびそれらの医薬用途 |
Country Status (9)
| Country | Link |
|---|---|
| EP (1) | EP1419177B1 (enExample) |
| JP (1) | JP2005508892A (enExample) |
| AT (1) | ATE393780T1 (enExample) |
| AU (1) | AU2002321012B2 (enExample) |
| CA (1) | CA2456843A1 (enExample) |
| DE (1) | DE60226327T2 (enExample) |
| DK (1) | DK1419177T3 (enExample) |
| ES (1) | ES2305272T3 (enExample) |
| WO (1) | WO2003016348A2 (enExample) |
Cited By (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2012029954A1 (ja) | 2010-09-03 | 2012-03-08 | 国立大学法人徳島大学 | 新規Ｇｃグロブリンガラクトース脱糖体の製造方法 |
| JP2012532932A (ja) * | 2009-07-13 | 2012-12-20 | アラーガン、インコーポレイテッド | ボツリヌス神経毒素を得るためのプロセスおよびシステム |
| JP2013531623A (ja) * | 2010-05-18 | 2013-08-08 | アッヴィ・インコーポレイテッド | タンパク質の精製装置および方法 |
| WO2015087981A1 (ja) * | 2013-12-13 | 2015-06-18 | 医療法人再生未来 | ウシ初乳酵素処理物、その製造方法、組成物および飲食品 |
| WO2016194914A1 (ja) * | 2015-06-01 | 2016-12-08 | 再生ファーマ株式会社 | 乳酵素処理物、その製造方法、組成物および製品 |
Families Citing this family (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN101005859B (zh) * | 2004-06-29 | 2012-08-15 | 利莱恩斯生命科学有限公司 | 灭病毒生物液体的制备方法 |
| CN100354301C (zh) * | 2005-10-13 | 2007-12-12 | 南京工业大学 | 化学合成多肽的新型大规模分离制备技术 |
| EP2682168A1 (en) | 2012-07-02 | 2014-01-08 | Millipore Corporation | Purification of biological molecules |
| WO2015158776A1 (en) * | 2014-04-15 | 2015-10-22 | Boehringer Ingelheim International Gmbh | Methods, apparatuses, and systems for continuously inactivating a virus during manufacture of a biological product |
Family Cites Families (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5177002A (en) * | 1989-11-20 | 1993-01-05 | Nobuto Yamamoto | In vitro enzymatic conversion of glycosylated human vitamin D binding protein to a potent macrophage activating factor |
| ATE171625T1 (de) * | 1990-04-11 | 1998-10-15 | Brigham & Womens Hospital | Therapeutische verwendung von actin-bindenden verbindungen |
| US6268478B1 (en) * | 1996-02-12 | 2001-07-31 | Cedars-Sinai Medical Center | Intracellular vitamin D binding protein |
-
2002
- 2002-08-12 AT AT02754557T patent/ATE393780T1/de not_active IP Right Cessation
- 2002-08-12 AU AU2002321012A patent/AU2002321012B2/en not_active Ceased
- 2002-08-12 EP EP02754557A patent/EP1419177B1/en not_active Expired - Lifetime
- 2002-08-12 DK DK02754557T patent/DK1419177T3/da active
- 2002-08-12 WO PCT/DK2002/000531 patent/WO2003016348A2/en not_active Ceased
- 2002-08-12 ES ES02754557T patent/ES2305272T3/es not_active Expired - Lifetime
- 2002-08-12 CA CA002456843A patent/CA2456843A1/en not_active Abandoned
- 2002-08-12 JP JP2003521270A patent/JP2005508892A/ja not_active Withdrawn
- 2002-08-12 DE DE60226327T patent/DE60226327T2/de not_active Expired - Fee Related
Cited By (16)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2020078306A (ja) * | 2009-07-13 | 2020-05-28 | アラーガン、インコーポレイテッドＡｌｌｅｒｇａｎ，Ｉｎｃｏｒｐｏｒａｔｅｄ | ボツリヌス神経毒素を得るためのプロセスおよびシステム |
| JP2017070291A (ja) * | 2009-07-13 | 2017-04-13 | アラーガン、インコーポレイテッドＡｌｌｅｒｇａｎ，Ｉｎｃｏｒｐｏｒａｔｅｄ | ボツリヌス神経毒素を得るためのプロセスおよびシステム |
| JP2021193103A (ja) * | 2009-07-13 | 2021-12-23 | アラーガン、インコーポレイテッドAllergan, Incorporated | ボツリヌス神経毒素を得るためのプロセスおよびシステム |
| JP2012532932A (ja) * | 2009-07-13 | 2012-12-20 | アラーガン、インコーポレイテッド | ボツリヌス神経毒素を得るためのプロセスおよびシステム |
| JP2016028601A (ja) * | 2009-07-13 | 2016-03-03 | アラーガン、インコーポレイテッドＡｌｌｅｒｇａｎ，Ｉｎｃｏｒｐｏｒａｔｅｄ | ボツリヌス神経毒素を得るためのプロセスおよびシステム |
| JP2017002049A (ja) * | 2010-05-18 | 2017-01-05 | アッヴィ・インコーポレイテッド | タンパク質の精製装置および方法 |
| JP2013531623A (ja) * | 2010-05-18 | 2013-08-08 | アッヴィ・インコーポレイテッド | タンパク質の精製装置および方法 |
| WO2012029954A1 (ja) | 2010-09-03 | 2012-03-08 | 国立大学法人徳島大学 | 新規Ｇｃグロブリンガラクトース脱糖体の製造方法 |
| KR20160096089A (ko) * | 2013-12-13 | 2016-08-12 | 사이세이 파마 씨오., 엘티디. | 소 초유 효소 처리물, 그 제조방법, 조성물 및 식품 |
| WO2015087981A1 (ja) * | 2013-12-13 | 2015-06-18 | 医療法人再生未来 | ウシ初乳酵素処理物、その製造方法、組成物および飲食品 |
| JPWO2015087981A1 (ja) * | 2013-12-13 | 2017-03-16 | 再生ファーマ株式会社 | ウシ初乳酵素処理物、その製造方法、組成物および飲食品 |
| US10322147B2 (en) | 2013-12-13 | 2019-06-18 | Saisei Pharma Co., Ltd. | Enzyme-treated bovine colostrum, preparation method thereof, composition, and foods and beverages |
| KR102309707B1 (ko) * | 2013-12-13 | 2021-10-06 | 사이세이 파마 씨오., 엘티디. | 소 초유 효소 처리물, 그 제조방법, 조성물 및 식품 |
| WO2016194914A1 (ja) * | 2015-06-01 | 2016-12-08 | 再生ファーマ株式会社 | 乳酵素処理物、その製造方法、組成物および製品 |
| JPWO2016194914A1 (ja) * | 2015-06-01 | 2018-04-26 | 再生ファーマ株式会社 | 乳酵素処理物、その製造方法、組成物および製品 |
| JP2022009514A (ja) * | 2015-06-01 | 2022-01-14 | 再生ファーマ株式会社 | 乳酵素処理物、その製造方法、組成物および製品 |
Also Published As
| Publication number | Publication date |
|---|---|
| DE60226327D1 (de) | 2008-06-12 |
| DK1419177T3 (da) | 2008-08-25 |
| AU2002321012B2 (en) | 2008-07-24 |
| WO2003016348A2 (en) | 2003-02-27 |
| ATE393780T1 (de) | 2008-05-15 |
| WO2003016348A3 (en) | 2004-03-04 |
| EP1419177A2 (en) | 2004-05-19 |
| DE60226327T2 (de) | 2009-07-09 |
| EP1419177B1 (en) | 2008-04-30 |
| CA2456843A1 (en) | 2003-02-27 |
| ES2305272T3 (es) | 2008-11-01 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US6806355B2 (en) | Purification process for large scale production of Gc-globulin, the Gc-globulin produced hereby, a use of Gc.globulin and a Gc-globulin medicinal product | |
| US6281336B1 (en) | Process for producing immunoglobulins for intravenous administration and other immunoglobulin products | |
| EP1084147B1 (en) | Process for producing immunoglobulins for intravenous administration and other immunoglobulin products | |
| JP6876655B2 (ja) | タンパク質の精製方法 | |
| JPH09509165A (ja) | ミルクからのラクトフェリンの分離 | |
| CN103153333B (zh) | 补体因子h的纯化方法 | |
| EP1419177B1 (en) | A purification process for large scale production of gc-globulin, product obtained thereby and their use in medicine | |
| PL165402B1 (pl) | Sposób wydzielania oczyszczonego roztworu albuminy PL | |
| AU2002321012A1 (en) | A purification process for large scale production of Gc-globulin, product obtained thereby and their use in medicine | |
| Marmorstein et al. | Epithelial permeability factor: a serum protein that condenses actin and opens tight junctions | |
| US9145448B2 (en) | Method for the isolation of haptoglobin | |
| Lee | Joergensen et al. | |
| HK1151044B (en) | Process for manufacturing immunoglobulins for intravenous administration and other immunoglobulin-like products | |
| HK1151045B (en) | Liquid immunoglobulin g (lgg) product | |
| JPH02157298A (ja) | 新規補体制御物質 | |
| JPH1036396A (ja) | 高純度トランスサイレチン含有組成物の製造方法、高純度トランスサイレチン含有組成物および異型トランスサイレチン分泌抑制用組成物 | |
| MXPA00012230A (en) | Process for producing immunoglobulins for intravenous administration and other immunoglobulin products |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20050805 |
|
| A621 | Written request for application examination |
Free format text: JAPANESE INTERMEDIATE CODE: A621 Effective date: 20050805 |
|
| A761 | Written withdrawal of application |
Free format text: JAPANESE INTERMEDIATE CODE: A761 Effective date: 20070718 |