CN112717125A - 一种纯化蛋白质的方法 - Google Patents
一种纯化蛋白质的方法 Download PDFInfo
- Publication number
- CN112717125A CN112717125A CN202110206879.5A CN202110206879A CN112717125A CN 112717125 A CN112717125 A CN 112717125A CN 202110206879 A CN202110206879 A CN 202110206879A CN 112717125 A CN112717125 A CN 112717125A
- Authority
- CN
- China
- Prior art keywords
- haptoglobin
- hemopexin
- composition
- pharmaceutical composition
- transferrin
- 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.)
- Pending
Links
- 238000000034 method Methods 0.000 title claims abstract description 90
- 102000004169 proteins and genes Human genes 0.000 title claims abstract description 79
- 108090000623 proteins and genes Proteins 0.000 title claims abstract description 79
- 102000014702 Haptoglobin Human genes 0.000 claims abstract description 154
- 108050005077 Haptoglobin Proteins 0.000 claims abstract description 154
- 102000013271 Hemopexin Human genes 0.000 claims abstract description 135
- 108010026027 Hemopexin Proteins 0.000 claims abstract description 135
- 239000000203 mixture Substances 0.000 claims description 99
- 102000004338 Transferrin Human genes 0.000 claims description 79
- 108090000901 Transferrin Proteins 0.000 claims description 79
- 239000012581 transferrin Substances 0.000 claims description 79
- 239000008194 pharmaceutical composition Substances 0.000 claims description 29
- 206010018910 Haemolysis Diseases 0.000 claims description 18
- 230000008588 hemolysis Effects 0.000 claims description 18
- 239000003599 detergent Substances 0.000 claims description 14
- 102000009027 Albumins Human genes 0.000 claims description 11
- 108010088751 Albumins Proteins 0.000 claims description 11
- 241000700605 Viruses Species 0.000 claims description 10
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 claims description 10
- 239000002904 solvent Substances 0.000 claims description 9
- 239000003814 drug Substances 0.000 claims description 8
- 238000002360 preparation method Methods 0.000 claims description 8
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 claims description 7
- 239000003381 stabilizer Substances 0.000 claims description 6
- 102100033312 Alpha-2-macroglobulin Human genes 0.000 claims description 5
- 108010015078 Pregnancy-Associated alpha 2-Macroglobulins Proteins 0.000 claims description 5
- 208000035475 disorder Diseases 0.000 claims description 5
- 208000007502 anemia Diseases 0.000 claims description 4
- 239000003937 drug carrier Substances 0.000 claims description 4
- 229940124597 therapeutic agent Drugs 0.000 claims description 4
- 208000023275 Autoimmune disease Diseases 0.000 claims description 3
- 102100036050 Phosphatidylinositol N-acetylglucosaminyltransferase subunit A Human genes 0.000 claims description 3
- OEUUFNIKLCFNLN-LLVKDONJSA-N chembl432481 Chemical group OC(=O)[C@@]1(C)CSC(C=2C(=CC(O)=CC=2)O)=N1 OEUUFNIKLCFNLN-LLVKDONJSA-N 0.000 claims description 3
- 208000009601 hereditary spherocytosis Diseases 0.000 claims description 3
- 201000003045 paroxysmal nocturnal hemoglobinuria Diseases 0.000 claims description 3
- 239000000546 pharmaceutical excipient Substances 0.000 claims description 3
- 230000009467 reduction Effects 0.000 claims description 3
- 208000007056 sickle cell anemia Diseases 0.000 claims description 3
- 208000010839 B-cell chronic lymphocytic leukemia Diseases 0.000 claims description 2
- 208000035220 Dyserythropoietic Congenital Anemia Diseases 0.000 claims description 2
- TZXKOCQBRNJULO-UHFFFAOYSA-N Ferriprox Chemical compound CC1=C(O)C(=O)C=CN1C TZXKOCQBRNJULO-UHFFFAOYSA-N 0.000 claims description 2
- 208000032759 Hemolytic-Uremic Syndrome Diseases 0.000 claims description 2
- 208000031422 Lymphocytic Chronic B-Cell Leukemia Diseases 0.000 claims description 2
- UBQYURCVBFRUQT-UHFFFAOYSA-N N-benzoyl-Ferrioxamine B Chemical group CC(=O)N(O)CCCCCNC(=O)CCC(=O)N(O)CCCCCNC(=O)CCC(=O)N(O)CCCCCN UBQYURCVBFRUQT-UHFFFAOYSA-N 0.000 claims description 2
- 208000000733 Paroxysmal Hemoglobinuria Diseases 0.000 claims description 2
- 208000002903 Thalassemia Diseases 0.000 claims description 2
- 208000032852 chronic lymphocytic leukemia Diseases 0.000 claims description 2
- 201000004440 congenital dyserythropoietic anemia Diseases 0.000 claims description 2
- 229960003266 deferiprone Drugs 0.000 claims description 2
- 229960000958 deferoxamine Drugs 0.000 claims description 2
- 239000003085 diluting agent Substances 0.000 claims description 2
- 208000007475 hemolytic anemia Diseases 0.000 claims description 2
- 208000015181 infectious disease Diseases 0.000 claims description 2
- 238000001802 infusion Methods 0.000 claims description 2
- 208000014674 injury Diseases 0.000 claims description 2
- 201000004792 malaria Diseases 0.000 claims description 2
- 201000000596 systemic lupus erythematosus Diseases 0.000 claims description 2
- 230000008733 trauma Effects 0.000 claims description 2
- 238000001728 nano-filtration Methods 0.000 claims 1
- 238000004848 nephelometry Methods 0.000 claims 1
- 239000007858 starting material Substances 0.000 abstract description 32
- 239000000243 solution Substances 0.000 description 92
- 239000000872 buffer Substances 0.000 description 63
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 52
- RAXXELZNTBOGNW-UHFFFAOYSA-N imidazole Natural products C1=CNC=N1 RAXXELZNTBOGNW-UHFFFAOYSA-N 0.000 description 42
- 239000011347 resin Substances 0.000 description 42
- 229920005989 resin Polymers 0.000 description 42
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 40
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 40
- 235000011130 ammonium sulphate Nutrition 0.000 description 40
- 239000012539 chromatography resin Substances 0.000 description 31
- 239000002244 precipitate Substances 0.000 description 31
- 239000011780 sodium chloride Substances 0.000 description 26
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 23
- 239000001632 sodium acetate Substances 0.000 description 23
- 235000017281 sodium acetate Nutrition 0.000 description 23
- 239000007983 Tris buffer Substances 0.000 description 22
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 21
- 238000000746 purification Methods 0.000 description 21
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 21
- 150000003278 haem Chemical class 0.000 description 18
- 150000002632 lipids Chemical class 0.000 description 18
- 238000009472 formulation Methods 0.000 description 17
- 238000001914 filtration Methods 0.000 description 16
- 238000011068 loading method Methods 0.000 description 16
- 238000005571 anion exchange chromatography Methods 0.000 description 15
- 239000000284 extract Substances 0.000 description 15
- 238000011026 diafiltration Methods 0.000 description 14
- 239000000706 filtrate Substances 0.000 description 14
- 238000004191 hydrophobic interaction chromatography Methods 0.000 description 14
- 239000012535 impurity Substances 0.000 description 13
- 239000012528 membrane Substances 0.000 description 13
- 238000000605 extraction Methods 0.000 description 12
- 239000001488 sodium phosphate Substances 0.000 description 12
- 229910000162 sodium phosphate Inorganic materials 0.000 description 12
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 12
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 12
- 229910002012 Aerosil® Inorganic materials 0.000 description 11
- 230000027455 binding Effects 0.000 description 11
- 239000003795 chemical substances by application Substances 0.000 description 11
- 239000011536 extraction buffer Substances 0.000 description 11
- 125000002347 octyl group Chemical group [H]C([*])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])[H] 0.000 description 10
- 230000001376 precipitating effect Effects 0.000 description 10
- GUPXYSSGJWIURR-UHFFFAOYSA-N 3-octoxypropane-1,2-diol Chemical compound CCCCCCCCOCC(O)CO GUPXYSSGJWIURR-UHFFFAOYSA-N 0.000 description 9
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 9
- 150000001413 amino acids Chemical class 0.000 description 9
- 239000001166 ammonium sulphate Substances 0.000 description 9
- 239000006167 equilibration buffer Substances 0.000 description 9
- XEEYBQQBJWHFJM-UHFFFAOYSA-N Iron Chemical compound [Fe] XEEYBQQBJWHFJM-UHFFFAOYSA-N 0.000 description 8
- 239000013622 capto Q Substances 0.000 description 8
- 238000004587 chromatography analysis Methods 0.000 description 8
- 238000010790 dilution Methods 0.000 description 8
- 239000012895 dilution Substances 0.000 description 8
- 239000012149 elution buffer Substances 0.000 description 8
- 230000002779 inactivation Effects 0.000 description 8
- 229910021645 metal ion Inorganic materials 0.000 description 8
- 230000008569 process Effects 0.000 description 8
- 239000008215 water for injection Substances 0.000 description 8
- 238000011210 chromatographic step Methods 0.000 description 7
- 238000011067 equilibration Methods 0.000 description 7
- 229910021485 fumed silica Inorganic materials 0.000 description 7
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 6
- 239000003153 chemical reaction reagent Substances 0.000 description 6
- 238000011033 desalting Methods 0.000 description 6
- 238000013400 design of experiment Methods 0.000 description 6
- 230000000694 effects Effects 0.000 description 6
- 238000000108 ultra-filtration Methods 0.000 description 6
- 230000003612 virological effect Effects 0.000 description 6
- 229920000936 Agarose Polymers 0.000 description 5
- 102000004506 Blood Proteins Human genes 0.000 description 5
- 108010017384 Blood Proteins Proteins 0.000 description 5
- 102000001554 Hemoglobins Human genes 0.000 description 5
- 108010054147 Hemoglobins Proteins 0.000 description 5
- 241001465754 Metazoa Species 0.000 description 5
- 238000001042 affinity chromatography Methods 0.000 description 5
- 239000003957 anion exchange resin Substances 0.000 description 5
- 210000004369 blood Anatomy 0.000 description 5
- 239000008280 blood Substances 0.000 description 5
- -1 diethylaminopropyl groups Chemical group 0.000 description 5
- 238000010828 elution Methods 0.000 description 5
- 238000005194 fractionation Methods 0.000 description 5
- 238000004108 freeze drying Methods 0.000 description 5
- 239000000499 gel Substances 0.000 description 5
- 102000028546 heme binding Human genes 0.000 description 5
- 108091022907 heme binding Proteins 0.000 description 5
- 238000001556 precipitation Methods 0.000 description 5
- 238000002305 strong-anion-exchange chromatography Methods 0.000 description 5
- 239000000725 suspension Substances 0.000 description 5
- 102000004411 Antithrombin III Human genes 0.000 description 4
- 108090000935 Antithrombin III Proteins 0.000 description 4
- 102000005666 Apolipoprotein A-I Human genes 0.000 description 4
- 108010059886 Apolipoprotein A-I Proteins 0.000 description 4
- 101710095342 Apolipoprotein B Proteins 0.000 description 4
- 102100040202 Apolipoprotein B-100 Human genes 0.000 description 4
- 108010075016 Ceruloplasmin Proteins 0.000 description 4
- 102100023321 Ceruloplasmin Human genes 0.000 description 4
- 241000283086 Equidae Species 0.000 description 4
- 239000000020 Nitrocellulose Substances 0.000 description 4
- 108010061952 Orosomucoid Proteins 0.000 description 4
- 102000012404 Orosomucoid Human genes 0.000 description 4
- 102000007584 Prealbumin Human genes 0.000 description 4
- 108010071690 Prealbumin Proteins 0.000 description 4
- MZVQCMJNVPIDEA-UHFFFAOYSA-N [CH2]CN(CC)CC Chemical compound [CH2]CN(CC)CC MZVQCMJNVPIDEA-UHFFFAOYSA-N 0.000 description 4
- 108010050122 alpha 1-Antitrypsin Proteins 0.000 description 4
- 102000015395 alpha 1-Antitrypsin Human genes 0.000 description 4
- 229940024142 alpha 1-antitrypsin Drugs 0.000 description 4
- 238000005349 anion exchange Methods 0.000 description 4
- 229960005348 antithrombin iii Drugs 0.000 description 4
- 230000003139 buffering effect Effects 0.000 description 4
- 239000012501 chromatography medium Substances 0.000 description 4
- 238000010586 diagram Methods 0.000 description 4
- 238000001962 electrophoresis Methods 0.000 description 4
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 4
- 230000002209 hydrophobic effect Effects 0.000 description 4
- 229910052742 iron Inorganic materials 0.000 description 4
- 229920001220 nitrocellulos Polymers 0.000 description 4
- 239000003960 organic solvent Substances 0.000 description 4
- 125000001453 quaternary ammonium group Chemical group 0.000 description 4
- 150000003839 salts Chemical class 0.000 description 4
- 238000000926 separation method Methods 0.000 description 4
- 239000007787 solid Substances 0.000 description 4
- AXAVXPMQTGXXJZ-UHFFFAOYSA-N 2-aminoacetic acid;2-amino-2-(hydroxymethyl)propane-1,3-diol Chemical compound NCC(O)=O.OCC(N)(CO)CO AXAVXPMQTGXXJZ-UHFFFAOYSA-N 0.000 description 3
- 239000004475 Arginine Substances 0.000 description 3
- 239000004471 Glycine Substances 0.000 description 3
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 3
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 3
- 241000288906 Primates Species 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 229930006000 Sucrose Natural products 0.000 description 3
- 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 3
- 238000012870 ammonium sulfate precipitation Methods 0.000 description 3
- 238000004458 analytical method Methods 0.000 description 3
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 3
- 238000005119 centrifugation Methods 0.000 description 3
- 150000001875 compounds Chemical class 0.000 description 3
- 239000012141 concentrate Substances 0.000 description 3
- 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 3
- 210000003743 erythrocyte Anatomy 0.000 description 3
- 230000003993 interaction Effects 0.000 description 3
- 238000004255 ion exchange chromatography Methods 0.000 description 3
- 239000002609 medium Substances 0.000 description 3
- 238000009928 pasteurization Methods 0.000 description 3
- 239000008188 pellet Substances 0.000 description 3
- 239000002953 phosphate buffered saline Substances 0.000 description 3
- 229920000642 polymer Polymers 0.000 description 3
- 229920000053 polysorbate 80 Polymers 0.000 description 3
- 239000000843 powder Substances 0.000 description 3
- 238000011084 recovery Methods 0.000 description 3
- 230000000717 retained effect Effects 0.000 description 3
- 239000005720 sucrose Substances 0.000 description 3
- 235000000346 sugar Nutrition 0.000 description 3
- 150000005846 sugar alcohols Chemical class 0.000 description 3
- 150000008163 sugars Chemical class 0.000 description 3
- 238000011100 viral filtration Methods 0.000 description 3
- 238000004271 weak anion exchange chromatography Methods 0.000 description 3
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 2
- 229910002019 Aerosil® 380 Inorganic materials 0.000 description 2
- NLXLAEXVIDQMFP-UHFFFAOYSA-N Ammonia chloride Chemical compound [NH4+].[Cl-] NLXLAEXVIDQMFP-UHFFFAOYSA-N 0.000 description 2
- 241000283707 Capra Species 0.000 description 2
- FBPFZTCFMRRESA-KVTDHHQDSA-N D-Mannitol Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-KVTDHHQDSA-N 0.000 description 2
- 241000282412 Homo Species 0.000 description 2
- 101001078385 Homo sapiens Haptoglobin Proteins 0.000 description 2
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 2
- 229930195725 Mannitol Natural products 0.000 description 2
- PXHVJJICTQNCMI-UHFFFAOYSA-N Nickel Chemical compound [Ni] PXHVJJICTQNCMI-UHFFFAOYSA-N 0.000 description 2
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 2
- 239000003463 adsorbent Substances 0.000 description 2
- 238000002617 apheresis Methods 0.000 description 2
- 239000007864 aqueous solution Substances 0.000 description 2
- 230000008901 benefit Effects 0.000 description 2
- 239000007853 buffer solution Substances 0.000 description 2
- 125000000484 butyl group Chemical group [H]C([*])([H])C([H])([H])C([H])([H])C([H])([H])[H] 0.000 description 2
- 230000002612 cardiopulmonary effect Effects 0.000 description 2
- 230000001413 cellular effect Effects 0.000 description 2
- 238000011097 chromatography purification Methods 0.000 description 2
- 230000006378 damage Effects 0.000 description 2
- 238000013461 design Methods 0.000 description 2
- 238000001514 detection method Methods 0.000 description 2
- 201000010099 disease Diseases 0.000 description 2
- 238000009826 distribution Methods 0.000 description 2
- 239000002552 dosage form Substances 0.000 description 2
- 239000003480 eluent Substances 0.000 description 2
- 238000010438 heat treatment Methods 0.000 description 2
- 230000002949 hemolytic effect Effects 0.000 description 2
- 102000050796 human HP Human genes 0.000 description 2
- 238000000338 in vitro Methods 0.000 description 2
- 125000005647 linker group Chemical group 0.000 description 2
- 239000012931 lyophilized formulation Substances 0.000 description 2
- 239000000594 mannitol Substances 0.000 description 2
- 235000010355 mannitol Nutrition 0.000 description 2
- 238000004519 manufacturing process Methods 0.000 description 2
- 238000002156 mixing Methods 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 238000010979 pH adjustment Methods 0.000 description 2
- 239000006174 pH buffer Substances 0.000 description 2
- 125000001997 phenyl group Chemical group [H]C1=C([H])C([H])=C(*)C([H])=C1[H] 0.000 description 2
- 239000000244 polyoxyethylene sorbitan monooleate Substances 0.000 description 2
- 235000010482 polyoxyethylene sorbitan monooleate Nutrition 0.000 description 2
- 229920000136 polysorbate Polymers 0.000 description 2
- 229950008882 polysorbate Drugs 0.000 description 2
- 229940068968 polysorbate 80 Drugs 0.000 description 2
- 108090000765 processed proteins & peptides Proteins 0.000 description 2
- 239000000047 product Substances 0.000 description 2
- 239000002516 radical scavenger Substances 0.000 description 2
- 239000003642 reactive oxygen metabolite Substances 0.000 description 2
- 239000000523 sample Substances 0.000 description 2
- 239000007974 sodium acetate buffer Substances 0.000 description 2
- JHJLBTNAGRQEKS-UHFFFAOYSA-M sodium bromide Chemical compound [Na+].[Br-] JHJLBTNAGRQEKS-UHFFFAOYSA-M 0.000 description 2
- 238000001179 sorption measurement Methods 0.000 description 2
- 238000001356 surgical procedure Methods 0.000 description 2
- 231100000331 toxic Toxicity 0.000 description 2
- 230000002588 toxic effect Effects 0.000 description 2
- 231100000419 toxicity Toxicity 0.000 description 2
- 230000001988 toxicity Effects 0.000 description 2
- 238000001262 western blot Methods 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
- 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 1
- IHPYMWDTONKSCO-UHFFFAOYSA-N 2,2'-piperazine-1,4-diylbisethanesulfonic acid Chemical compound OS(=O)(=O)CCN1CCN(CCS(O)(=O)=O)CC1 IHPYMWDTONKSCO-UHFFFAOYSA-N 0.000 description 1
- NUFBIAUZAMHTSP-UHFFFAOYSA-N 3-(n-morpholino)-2-hydroxypropanesulfonic acid Chemical compound OS(=O)(=O)CC(O)CN1CCOCC1 NUFBIAUZAMHTSP-UHFFFAOYSA-N 0.000 description 1
- 239000007991 ACES buffer Substances 0.000 description 1
- 239000007988 ADA buffer Substances 0.000 description 1
- 102000003966 Alpha-1-microglobulin Human genes 0.000 description 1
- 101800001761 Alpha-1-microglobulin Proteins 0.000 description 1
- 239000007992 BES buffer Substances 0.000 description 1
- 101710125089 Bindin Proteins 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- KSFOVUSSGSKXFI-GAQDCDSVSA-N CC1=C/2NC(\C=C3/N=C(/C=C4\N\C(=C/C5=N/C(=C\2)/C(C=C)=C5C)C(C=C)=C4C)C(C)=C3CCC(O)=O)=C1CCC(O)=O Chemical compound CC1=C/2NC(\C=C3/N=C(/C=C4\N\C(=C/C5=N/C(=C\2)/C(C=C)=C5C)C(C=C)=C4C)C(C)=C3CCC(O)=O)=C1CCC(O)=O KSFOVUSSGSKXFI-GAQDCDSVSA-N 0.000 description 1
- 241000282832 Camelidae Species 0.000 description 1
- 241000282472 Canis lupus familiaris Species 0.000 description 1
- 108010032608 Cohn fraction IV Proteins 0.000 description 1
- 241000777300 Congiopodidae Species 0.000 description 1
- RYGMFSIKBFXOCR-UHFFFAOYSA-N Copper Chemical compound [Cu] RYGMFSIKBFXOCR-UHFFFAOYSA-N 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
- 229920002307 Dextran Polymers 0.000 description 1
- 241000194033 Enterococcus Species 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 241000283074 Equus asinus Species 0.000 description 1
- 241000282326 Felis catus Species 0.000 description 1
- 230000005526 G1 to G0 transition Effects 0.000 description 1
- 208000025499 G6PD deficiency Diseases 0.000 description 1
- 102000006395 Globulins Human genes 0.000 description 1
- 108010044091 Globulins Proteins 0.000 description 1
- 102000003886 Glycoproteins Human genes 0.000 description 1
- 108090000288 Glycoproteins Proteins 0.000 description 1
- 206010018901 Haemoglobinaemia Diseases 0.000 description 1
- 102100034629 Hemopexin Human genes 0.000 description 1
- 101001067323 Homo sapiens Hemopexin Proteins 0.000 description 1
- 101000766306 Homo sapiens Serotransferrin Proteins 0.000 description 1
- 208000026350 Inborn Genetic disease Diseases 0.000 description 1
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 description 1
- 239000007993 MOPS buffer Substances 0.000 description 1
- 208000024556 Mendelian disease Diseases 0.000 description 1
- 102100030856 Myoglobin Human genes 0.000 description 1
- 108010062374 Myoglobin Proteins 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 239000007990 PIPES buffer Substances 0.000 description 1
- 208000030852 Parasitic disease Diseases 0.000 description 1
- 241001494479 Pecora Species 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 241000224016 Plasmodium Species 0.000 description 1
- 239000004952 Polyamide Substances 0.000 description 1
- 229920001213 Polysorbate 20 Polymers 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
- 239000012722 SDS sample buffer Substances 0.000 description 1
- 239000012507 Sephadex™ Substances 0.000 description 1
- 229920002684 Sepharose Polymers 0.000 description 1
- PMZURENOXWZQFD-UHFFFAOYSA-L Sodium Sulfate Chemical compound [Na+].[Na+].[O-]S([O-])(=O)=O PMZURENOXWZQFD-UHFFFAOYSA-L 0.000 description 1
- 206010041660 Splenomegaly Diseases 0.000 description 1
- 241000191940 Staphylococcus Species 0.000 description 1
- 241000194017 Streptococcus Species 0.000 description 1
- 241000282887 Suidae Species 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
- 239000013504 Triton X-100 Substances 0.000 description 1
- 229920004890 Triton X-100 Polymers 0.000 description 1
- 206010052428 Wound Diseases 0.000 description 1
- 208000027418 Wounds and injury Diseases 0.000 description 1
- HCHKCACWOHOZIP-UHFFFAOYSA-N Zinc Chemical compound [Zn] HCHKCACWOHOZIP-UHFFFAOYSA-N 0.000 description 1
- 230000002159 abnormal effect Effects 0.000 description 1
- 230000005856 abnormality Effects 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- 229960000583 acetic acid Drugs 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 150000001252 acrylic acid derivatives Chemical class 0.000 description 1
- 230000001154 acute effect Effects 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
- 235000019270 ammonium chloride Nutrition 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 230000000843 anti-fungal effect Effects 0.000 description 1
- 239000003146 anticoagulant agent Substances 0.000 description 1
- 229940127219 anticoagulant drug Drugs 0.000 description 1
- 239000003429 antifungal agent Substances 0.000 description 1
- 229940121375 antifungal agent Drugs 0.000 description 1
- 239000012148 binding buffer Substances 0.000 description 1
- 230000031018 biological processes and functions Effects 0.000 description 1
- 239000006172 buffering agent Substances 0.000 description 1
- 150000001720 carbohydrates Chemical class 0.000 description 1
- 235000014633 carbohydrates Nutrition 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- 230000030833 cell death Effects 0.000 description 1
- 230000006037 cell lysis Effects 0.000 description 1
- 239000001913 cellulose Substances 0.000 description 1
- 229920002678 cellulose Polymers 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 238000013375 chromatographic separation Methods 0.000 description 1
- 230000001684 chronic effect Effects 0.000 description 1
- 229910017052 cobalt Inorganic materials 0.000 description 1
- 239000010941 cobalt Substances 0.000 description 1
- GUTLYIVDDKVIGB-UHFFFAOYSA-N cobalt atom Chemical compound [Co] GUTLYIVDDKVIGB-UHFFFAOYSA-N 0.000 description 1
- 230000001447 compensatory effect Effects 0.000 description 1
- 239000008139 complexing agent Substances 0.000 description 1
- 239000002131 composite material Substances 0.000 description 1
- 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 1
- 229910052802 copper Inorganic materials 0.000 description 1
- 239000010949 copper Substances 0.000 description 1
- 238000010908 decantation Methods 0.000 description 1
- 230000007812 deficiency Effects 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 238000011118 depth filtration Methods 0.000 description 1
- 238000010612 desalination reaction Methods 0.000 description 1
- 238000007865 diluting Methods 0.000 description 1
- 239000000539 dimer Substances 0.000 description 1
- 239000002612 dispersion medium Substances 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 150000002170 ethers Chemical class 0.000 description 1
- 229920001038 ethylene copolymer Polymers 0.000 description 1
- 238000001704 evaporation Methods 0.000 description 1
- 230000008020 evaporation Effects 0.000 description 1
- 230000007717 exclusion Effects 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 230000004907 flux Effects 0.000 description 1
- 238000007710 freezing Methods 0.000 description 1
- 230000008014 freezing Effects 0.000 description 1
- 239000012362 glacial acetic acid Substances 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- 208000008605 glucosephosphate dehydrogenase deficiency Diseases 0.000 description 1
- 208000027136 gram-positive bacterial infections Diseases 0.000 description 1
- 208000034737 hemoglobinopathy Diseases 0.000 description 1
- 201000001505 hemoglobinuria Diseases 0.000 description 1
- 210000003494 hepatocyte Anatomy 0.000 description 1
- 125000001165 hydrophobic group Chemical group 0.000 description 1
- 239000012616 hydrophobic interaction chromatography medium Substances 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 239000012678 infectious agent Substances 0.000 description 1
- 239000007972 injectable composition Substances 0.000 description 1
- 238000001361 intraarterial administration Methods 0.000 description 1
- 238000001990 intravenous administration Methods 0.000 description 1
- 239000003456 ion exchange resin Substances 0.000 description 1
- 229920003303 ion-exchange polymer Polymers 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- 238000011031 large-scale manufacturing process Methods 0.000 description 1
- 239000003446 ligand Substances 0.000 description 1
- 230000004576 lipid-binding Effects 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 210000004185 liver Anatomy 0.000 description 1
- 244000144972 livestock Species 0.000 description 1
- 239000013627 low molecular weight specie Substances 0.000 description 1
- 239000008176 lyophilized powder Substances 0.000 description 1
- 210000002540 macrophage Anatomy 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 229910052751 metal Inorganic materials 0.000 description 1
- 239000002184 metal Substances 0.000 description 1
- 238000012544 monitoring process Methods 0.000 description 1
- 239000000178 monomer Substances 0.000 description 1
- 229910052759 nickel Inorganic materials 0.000 description 1
- 230000009871 nonspecific binding Effects 0.000 description 1
- 239000002773 nucleotide Substances 0.000 description 1
- 125000003729 nucleotide group Chemical group 0.000 description 1
- 230000003204 osmotic effect Effects 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 230000001575 pathological effect Effects 0.000 description 1
- 230000004963 pathophysiological condition Effects 0.000 description 1
- 150000002978 peroxides Chemical class 0.000 description 1
- 239000000825 pharmaceutical preparation Substances 0.000 description 1
- 238000010587 phase diagram Methods 0.000 description 1
- 230000004962 physiological condition Effects 0.000 description 1
- 239000002504 physiological saline solution Substances 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 229920002647 polyamide Polymers 0.000 description 1
- 239000011148 porous material Substances 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
- 235000011151 potassium sulphates Nutrition 0.000 description 1
- 230000001737 promoting effect Effects 0.000 description 1
- XNSAINXGIQZQOO-SRVKXCTJSA-N protirelin Chemical compound NC(=O)[C@@H]1CCCN1C(=O)[C@@H](NC(=O)[C@H]1NC(=O)CC1)CC1=CN=CN1 XNSAINXGIQZQOO-SRVKXCTJSA-N 0.000 description 1
- 229950003776 protoporphyrin Drugs 0.000 description 1
- 239000002994 raw material Substances 0.000 description 1
- 230000004043 responsiveness Effects 0.000 description 1
- 150000003335 secondary amines Chemical group 0.000 description 1
- 229910002027 silica gel Inorganic materials 0.000 description 1
- 239000000741 silica gel Substances 0.000 description 1
- 229910052938 sodium sulfate Inorganic materials 0.000 description 1
- 235000011152 sodium sulphate Nutrition 0.000 description 1
- VGTPCRGMBIAPIM-UHFFFAOYSA-M sodium thiocyanate Chemical compound [Na+].[S-]C#N VGTPCRGMBIAPIM-UHFFFAOYSA-M 0.000 description 1
- 239000012439 solid excipient Substances 0.000 description 1
- 230000003381 solubilizing effect Effects 0.000 description 1
- 239000000600 sorbitol Substances 0.000 description 1
- 239000012192 staining solution Substances 0.000 description 1
- 125000004079 stearyl group Chemical group [H]C([*])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])[H] 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 239000012609 strong anion exchange resin Substances 0.000 description 1
- 238000007920 subcutaneous administration Methods 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 239000004094 surface-active agent Substances 0.000 description 1
- 150000003512 tertiary amines Chemical class 0.000 description 1
- 230000001225 therapeutic effect Effects 0.000 description 1
- 239000003053 toxin Substances 0.000 description 1
- 231100000765 toxin Toxicity 0.000 description 1
- 108700012359 toxins Proteins 0.000 description 1
- STCOOQWBFONSKY-UHFFFAOYSA-N tributyl phosphate Chemical compound CCCCOP(=O)(OCCCC)OCCCC STCOOQWBFONSKY-UHFFFAOYSA-N 0.000 description 1
- 239000011534 wash buffer Substances 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 239000012610 weak anion exchange resin Substances 0.000 description 1
- 229910052725 zinc Inorganic materials 0.000 description 1
- 239000011701 zinc Substances 0.000 description 1
Images
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/14—Extraction; Separation; Purification
- C07K1/30—Extraction; Separation; Purification by precipitation
-
- 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
- A61K38/1722—Plasma globulins, lactoglobulins
-
- 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
- A61K38/41—Porphyrin- or corrin-ring-containing peptides
- A61K38/42—Haemoglobins; Myoglobins
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P13/00—Drugs for disorders of the urinary system
- A61P13/02—Drugs for disorders of the urinary system of urine or of the urinary tract, e.g. urine acidifiers
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P13/00—Drugs for disorders of the urinary system
- A61P13/12—Drugs for disorders of the urinary system of the kidneys
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P17/00—Drugs for dermatological disorders
- A61P17/02—Drugs for dermatological disorders for treating wounds, ulcers, burns, scars, keloids, or the like
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P33/00—Antiparasitic agents
- A61P33/02—Antiprotozoals, e.g. for leishmaniasis, trichomoniasis, toxoplasmosis
- A61P33/06—Antimalarials
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
- A61P35/02—Antineoplastic agents specific for leukemia
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
- A61P37/06—Immunosuppressants, e.g. drugs for graft rejection
-
- 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
-
- 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
- A61P7/04—Antihaemorrhagics; Procoagulants; Haemostatic agents; Antifibrinolytic agents
-
- 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
- A61P7/06—Antianaemics
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/14—Extraction; Separation; Purification
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/14—Extraction; Separation; Purification
- C07K1/16—Extraction; Separation; Purification by chromatography
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/14—Extraction; Separation; Purification
- C07K1/16—Extraction; Separation; Purification by chromatography
- C07K1/18—Ion-exchange chromatography
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/14—Extraction; Separation; Purification
- C07K1/36—Extraction; Separation; Purification by a combination of two or more processes of different types
-
- 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
- C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
- C07K14/4717—Plasma globulins, lactoglobulin
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/795—Porphyrin- or corrin-ring-containing peptides
- C07K14/805—Haemoglobins; Myoglobins
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02A—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE
- Y02A50/00—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE in human health protection, e.g. against extreme weather
- Y02A50/30—Against vector-borne diseases, e.g. mosquito-borne, fly-borne, tick-borne or waterborne diseases whose impact is exacerbated by climate change
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Veterinary Medicine (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Public Health (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Genetics & Genomics (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- General Chemical & Material Sciences (AREA)
- Immunology (AREA)
- Gastroenterology & Hepatology (AREA)
- Analytical Chemistry (AREA)
- Hematology (AREA)
- Zoology (AREA)
- Diabetes (AREA)
- Epidemiology (AREA)
- Toxicology (AREA)
- Urology & Nephrology (AREA)
- Tropical Medicine & Parasitology (AREA)
- Marine Sciences & Fisheries (AREA)
- Transplantation (AREA)
- Dermatology (AREA)
- Oncology (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
Applications Claiming Priority (9)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US201261709342P | 2012-10-03 | 2012-10-03 | |
| US61/709,342 | 2012-10-03 | ||
| US13/803,525 US9534029B2 (en) | 2012-10-03 | 2013-03-14 | Method of purifying proteins |
| US13/803,525 | 2013-03-14 | ||
| AU2013203930A AU2013203930B2 (en) | 2012-10-03 | 2013-04-11 | A method of purifying proteins |
| AU2013203930 | 2013-04-11 | ||
| EP13170202.9 | 2013-06-03 | ||
| EP13170202 | 2013-06-03 | ||
| CN201380051960.4A CN104968676A (zh) | 2012-10-03 | 2013-10-01 | 一种纯化蛋白质的方法 |
Related Parent Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN201380051960.4A Division CN104968676A (zh) | 2012-10-03 | 2013-10-01 | 一种纯化蛋白质的方法 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CN112717125A true CN112717125A (zh) | 2021-04-30 |
Family
ID=52824845
Family Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN201380051960.4A Pending CN104968676A (zh) | 2012-10-03 | 2013-10-01 | 一种纯化蛋白质的方法 |
| CN202110206879.5A Pending CN112717125A (zh) | 2012-10-03 | 2013-10-01 | 一种纯化蛋白质的方法 |
Family Applications Before (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN201380051960.4A Pending CN104968676A (zh) | 2012-10-03 | 2013-10-01 | 一种纯化蛋白质的方法 |
Country Status (8)
| Country | Link |
|---|---|
| EP (1) | EP2904005A1 (ko) |
| JP (2) | JP6370792B2 (ko) |
| KR (2) | KR102125695B1 (ko) |
| CN (2) | CN104968676A (ko) |
| CA (2) | CA3129057C (ko) |
| HK (1) | HK1212995A1 (ko) |
| SG (1) | SG11201501921SA (ko) |
| WO (1) | WO2014055552A1 (ko) |
Families Citing this family (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP3334441B1 (en) * | 2015-08-13 | 2021-06-16 | Kamada Ltd. | Compositions derived from cohn fraction paste and use thereof |
| JPWO2017170597A1 (ja) * | 2016-03-29 | 2019-02-14 | 協和発酵キリン株式会社 | 血中でハプトグロビンに結合して多価の免疫複合体を形成する抗体を有効成分とする自己免疫疾患治療剤 |
| JP2020530027A (ja) * | 2017-08-08 | 2020-10-15 | ツェー・エス・エル・ベーリング・アクチエンゲゼルシャフト | ヘモペキシン製剤 |
| WO2019203302A1 (ja) * | 2018-04-18 | 2019-10-24 | 積水メディカル株式会社 | ヘモグロビン分析方法 |
| EP3968988A1 (en) | 2019-05-17 | 2022-03-23 | Universität Zürich | Haptoglobin for use in treating an adverse secondary neurological outcome following a haemorrhagic stroke |
| CN117136068A (zh) | 2021-02-01 | 2023-11-28 | 瑞士杰特贝林生物制品有限公司 | 治疗或预防出血性中风后不良继发性神经学后果的方法 |
| US20240034749A1 (en) * | 2021-02-04 | 2024-02-01 | Green Cross Corporation | Method for purification of hemopexin and haptoglobin |
| WO2024134608A1 (en) | 2022-12-22 | 2024-06-27 | Csl Behring Ag | Method of purifying hemopexin using mixed-mode chromatography |
Citations (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4129648A (en) * | 1977-11-21 | 1978-12-12 | Collier Harry O J | Method for reducing endogenous prostaglandin synthesis |
| WO1990012803A1 (en) * | 1989-04-14 | 1990-11-01 | Biogen, Inc. | Process for purifying a protein |
| US20050153875A1 (en) * | 2002-04-16 | 2005-07-14 | Shabtai Bauer | Ultrapure transferrin for pharmaceutical compositions |
| US20090281282A1 (en) * | 2004-10-19 | 2009-11-12 | Nhs Blood And Transplant | Method for the isolation of haptoglobin |
| CN101842121A (zh) * | 2007-08-23 | 2010-09-22 | 奥克塔法马有限公司 | 分离和纯化靶蛋白使其不含朊蛋白(PrPSC)的方法 |
| CN101985611A (zh) * | 2009-07-28 | 2011-03-16 | 基立福有限公司 | 包含来自Cohn分级分离阶段上清液的哺乳动物细胞培养基及其用途 |
| US20120122179A1 (en) * | 2009-02-19 | 2012-05-17 | Lfb Biotechnologies | Means for purifying a protein of blood plasma and methods for implementing same |
Family Cites Families (27)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB1426039A (en) * | 1973-11-15 | 1976-02-25 | Green Cross Corp | Haptoglobin in aqueous solution and process for tits preparation |
| JPS5337406B2 (ko) * | 1973-11-15 | 1978-10-09 | ||
| US4764369A (en) | 1983-07-14 | 1988-08-16 | New York Blood Center Inc. | Undenatured virus-free biologically active protein derivatives |
| US4540573A (en) | 1983-07-14 | 1985-09-10 | New York Blood Center, Inc. | Undenatured virus-free biologically active protein derivatives |
| JPS6317899A (ja) * | 1986-07-09 | 1988-01-25 | Green Cross Corp:The | ハプトグロビンの精製方法 |
| JPH01305036A (ja) * | 1988-05-31 | 1989-12-08 | Green Cross Corp:The | 血漿蛋白成分の加熱処理方法および血漿蛋白成分製剤 |
| US5138034A (en) * | 1989-07-12 | 1992-08-11 | The Green Cross Corporation | Method of fractionating plasma proteins |
| FR2672604B1 (fr) * | 1991-02-07 | 1995-05-05 | Pasteur Merieux Serums Vacc | Procede pour isoler de l'albumine humaine a partir du surnageant iv, notamment iv-4, ou de la fraction v de cohn ou d'un surnageant ou fraction analogue. |
| SE9301582D0 (sv) * | 1993-05-07 | 1993-05-07 | Kabi Pharmacia Ab | Purification of plasma proteins |
| DE19830914C1 (de) * | 1998-07-10 | 1999-06-24 | Centeon Pharma Gmbh | Verfahren zur Herstellung einer Proteinlösung |
| US6093804A (en) * | 1998-09-24 | 2000-07-25 | American National Red Cross | Method for purification of alpha-1 proteinase inhibitor |
| US6815181B2 (en) * | 2001-07-09 | 2004-11-09 | Applera Corporation | Nucleic acid molecules encoding human secreted hemopexin-related proteins |
| DE10211632A1 (de) | 2002-03-15 | 2003-10-09 | Aventis Behring Gmbh | Verfahren zur Abtrennung von Viren aus einer Proteinlösung durch Nanofiltration |
| DE10215315A1 (de) * | 2002-04-05 | 2003-11-20 | Aventis Behring Gmbh Intellect | Human-Transferrin zur Behandlung der Anaemia of Chronic Disease (ACD) und des funktionellen Eisenmangels |
| DE10261126A1 (de) | 2002-08-13 | 2004-03-04 | Aventis Behring Gmbh | Lagerungsstabile, flüssige Fibrinogen-Formulierung |
| JP2004224793A (ja) * | 2003-01-17 | 2004-08-12 | Research Corp Technologies Inc | 子宮内膜症の治療方法 |
| JP2004256463A (ja) * | 2003-02-26 | 2004-09-16 | Univ Waseda | 多形核白血球の細胞接着抑制剤及び細胞接着抑制方法 |
| US7291338B2 (en) * | 2005-03-09 | 2007-11-06 | Idexx Laboratories, Inc. | Method and device for detecting feline immunodeficiency virus |
| JP2009537812A (ja) * | 2006-05-15 | 2009-10-29 | デジラブ インコーポレーテッド | ２型糖尿病プリフォームのバイオマーカー、及び２型糖尿病プリフォームの存在又は不在を検出する方法 |
| CA2694854C (en) * | 2007-08-17 | 2016-09-27 | Csl Behring Gmbh | Methods for purification of alpha-1-antitrypsin and apolipoprotein a-i |
| KR101426039B1 (ko) * | 2008-09-11 | 2014-08-01 | 삼성테크윈 주식회사 | 얼굴/물체 인식을 위한 특징점 검출 장치 및 방법 |
| EP2236617A1 (en) * | 2009-03-31 | 2010-10-06 | Leukocare Ag | Methods of terminal sterilization of biofunctional compositions |
| WO2011002070A1 (ja) * | 2009-07-02 | 2011-01-06 | 協和発酵キリン株式会社 | Ｇｄｆ７／ｂｍｐ１２蛋白質を含有する鉄過剰疾患または鉄濃度を低下させることが有効な疾患に対する治療用医薬組成物 |
| WO2011007208A1 (en) * | 2009-07-16 | 2011-01-20 | Institut National De La Sante Et De La Recherche Medicale (Inserm) | Compounds and methods for the treatment of cancer |
| PT2464655T (pt) * | 2009-08-11 | 2017-05-25 | Biocon Ltd | Processos cromatográficos |
| AU2011244348B2 (en) * | 2010-04-20 | 2015-02-12 | Octapharma Ag | New stabilizing agent for pharmaceutical proteins |
| WO2012050874A2 (en) * | 2010-09-28 | 2012-04-19 | Soares Miguel P | Targeting heme for the treatment of immune mediated inflammatory diseases |
-
2013
- 2013-10-01 CN CN201380051960.4A patent/CN104968676A/zh active Pending
- 2013-10-01 CN CN202110206879.5A patent/CN112717125A/zh active Pending
- 2013-10-01 EP EP13777203.4A patent/EP2904005A1/en not_active Withdrawn
- 2013-10-01 CA CA3129057A patent/CA3129057C/en active Active
- 2013-10-01 SG SG11201501921SA patent/SG11201501921SA/en unknown
- 2013-10-01 WO PCT/US2013/062916 patent/WO2014055552A1/en active Application Filing
- 2013-10-01 KR KR1020157011544A patent/KR102125695B1/ko active IP Right Grant
- 2013-10-01 JP JP2015535745A patent/JP6370792B2/ja active Active
- 2013-10-01 CA CA2886726A patent/CA2886726C/en active Active
- 2013-10-01 KR KR1020207017157A patent/KR102231613B1/ko active IP Right Grant
-
2016
- 2016-01-26 HK HK16100830.6A patent/HK1212995A1/zh unknown
-
2018
- 2018-07-10 JP JP2018130335A patent/JP6876655B2/ja active Active
Patent Citations (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4129648A (en) * | 1977-11-21 | 1978-12-12 | Collier Harry O J | Method for reducing endogenous prostaglandin synthesis |
| WO1990012803A1 (en) * | 1989-04-14 | 1990-11-01 | Biogen, Inc. | Process for purifying a protein |
| US5169936A (en) * | 1989-04-14 | 1992-12-08 | Biogen, Inc. | Protein purification on immobilized metal affinity resins effected by elution using a weak ligand |
| US20050153875A1 (en) * | 2002-04-16 | 2005-07-14 | Shabtai Bauer | Ultrapure transferrin for pharmaceutical compositions |
| US20090281282A1 (en) * | 2004-10-19 | 2009-11-12 | Nhs Blood And Transplant | Method for the isolation of haptoglobin |
| CN101842121A (zh) * | 2007-08-23 | 2010-09-22 | 奥克塔法马有限公司 | 分离和纯化靶蛋白使其不含朊蛋白(PrPSC)的方法 |
| US20120122179A1 (en) * | 2009-02-19 | 2012-05-17 | Lfb Biotechnologies | Means for purifying a protein of blood plasma and methods for implementing same |
| CN101985611A (zh) * | 2009-07-28 | 2011-03-16 | 基立福有限公司 | 包含来自Cohn分级分离阶段上清液的哺乳动物细胞培养基及其用途 |
Non-Patent Citations (3)
| Title |
|---|
| ELENA A SHER等: "Hemopexin Is Protective Against Intravascular Hemolysis–Induced Vascular Damage", 《BLOOD》, vol. 116, no. 21, 19 November 2010 (2010-11-19), XP086607218, DOI: 10.1182/blood.V116.21.3207.3207 * |
| MARCIA R MAUK等: "Metal ion binding to human hemopexin", 《BIOCHEMISTRY》, vol. 44, no. 6, pages 1864 - 1865 * |
| N BERNARD等: "Isolation and physical chemical properties of rat hemopexin", 《BIOCHIMIE》, vol. 57, no. 5, pages 552 * |
Also Published As
| Publication number | Publication date |
|---|---|
| KR102125695B1 (ko) | 2020-06-24 |
| KR20200075027A (ko) | 2020-06-25 |
| CA3129057A1 (en) | 2014-04-10 |
| CA2886726C (en) | 2021-11-23 |
| KR20150063547A (ko) | 2015-06-09 |
| SG11201501921SA (en) | 2015-04-29 |
| CA3129057C (en) | 2023-03-07 |
| CN104968676A (zh) | 2015-10-07 |
| JP2018172426A (ja) | 2018-11-08 |
| JP6876655B2 (ja) | 2021-05-26 |
| KR102231613B1 (ko) | 2021-03-25 |
| CA2886726A1 (en) | 2014-04-10 |
| EP2904005A1 (en) | 2015-08-12 |
| JP2015532301A (ja) | 2015-11-09 |
| WO2014055552A1 (en) | 2014-04-10 |
| JP6370792B2 (ja) | 2018-08-08 |
| HK1212995A1 (zh) | 2016-06-24 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US10918696B2 (en) | Methods of treatment using hemopexin compositions | |
| JP6876655B2 (ja) | タンパク質の精製方法 | |
| CA2694854C (en) | Methods for purification of alpha-1-antitrypsin and apolipoprotein a-i | |
| EP3398964A1 (en) | Chromatographic method for isolating and purifying high-purity recombined human serum albumin | |
| JP6259777B2 (ja) | Ｉｇａの富化方法 | |
| JP2002517516A (ja) | 静脈投与用免疫グロブリン及び他の免疫グロブリン生成物の製造法 | |
| CA2584407C (en) | Method for the isolation of haptoglobin | |
| US20240010710A1 (en) | Method for obtaining a composition comprising human plasma-derived immunoglobulin m | |
| US20240034749A1 (en) | Method for purification of hemopexin and haptoglobin | |
| WO2024134608A1 (en) | Method of purifying hemopexin using mixed-mode chromatography | |
| AU2012213935B2 (en) | Methods for purification of alpha-1-antitrypsin and apolipoprotein A-1 |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| PB01 | Publication | ||
| PB01 | Publication | ||
| SE01 | Entry into force of request for substantive examination | ||
| SE01 | Entry into force of request for substantive examination | ||
| REG | Reference to a national code |
Ref country code: HK Ref legal event code: DE Ref document number: 40050028 Country of ref document: HK |