JP2006502098A - アルブミン精製法 - Google Patents
アルブミン精製法 Download PDFInfo
- Publication number
- JP2006502098A JP2006502098A JP2004506364A JP2004506364A JP2006502098A JP 2006502098 A JP2006502098 A JP 2006502098A JP 2004506364 A JP2004506364 A JP 2004506364A JP 2004506364 A JP2004506364 A JP 2004506364A JP 2006502098 A JP2006502098 A JP 2006502098A
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- Prior art keywords
- matrix
- rhsa
- ligand
- cation exchange
- ccs
- 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
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- 238000000034 method Methods 0.000 title claims abstract description 50
- 238000000746 purification Methods 0.000 title abstract description 16
- 102000009027 Albumins Human genes 0.000 title description 3
- 108010088751 Albumins Proteins 0.000 title description 3
- 239000011159 matrix material Substances 0.000 claims abstract description 70
- 238000004191 hydrophobic interaction chromatography Methods 0.000 claims abstract description 32
- 238000005341 cation exchange Methods 0.000 claims abstract description 22
- 108091006905 Human Serum Albumin Proteins 0.000 claims abstract description 18
- 102000008100 Human Serum Albumin Human genes 0.000 claims abstract description 18
- 230000002902 bimodal effect Effects 0.000 claims abstract description 13
- 239000012228 culture supernatant Substances 0.000 claims abstract description 10
- 238000004113 cell culture Methods 0.000 claims abstract description 9
- 230000015784 hyperosmotic salinity response Effects 0.000 claims abstract description 6
- 238000005349 anion exchange Methods 0.000 claims abstract description 5
- 239000003446 ligand Substances 0.000 claims description 51
- 150000001450 anions Chemical class 0.000 claims description 11
- 125000001997 phenyl group Chemical group [H]C1=C([H])C([H])=C(*)C([H])=C1[H] 0.000 claims description 11
- 230000003993 interaction Effects 0.000 claims description 9
- 239000001257 hydrogen Substances 0.000 claims description 8
- 229910052739 hydrogen Inorganic materials 0.000 claims description 8
- 230000002209 hydrophobic effect Effects 0.000 claims description 8
- 239000003638 chemical reducing agent Substances 0.000 claims description 4
- 238000011210 chromatographic step Methods 0.000 claims description 4
- 125000001931 aliphatic group Chemical group 0.000 claims 1
- 125000000623 heterocyclic group Chemical group 0.000 claims 1
- 239000000243 solution Substances 0.000 abstract description 8
- 238000010790 dilution Methods 0.000 abstract description 4
- 239000012895 dilution Substances 0.000 abstract description 4
- 150000001768 cations Chemical class 0.000 description 24
- 150000003839 salts Chemical class 0.000 description 18
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 12
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 12
- 239000012619 Butyl Sepharose® Substances 0.000 description 11
- 229920000936 Agarose Polymers 0.000 description 10
- 229920002684 Sepharose Polymers 0.000 description 10
- 239000000523 sample Substances 0.000 description 10
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- 239000000463 material Substances 0.000 description 9
- MYRTYDVEIRVNKP-UHFFFAOYSA-N 1,2-Divinylbenzene Chemical compound C=CC1=CC=CC=C1C=C MYRTYDVEIRVNKP-UHFFFAOYSA-N 0.000 description 8
- 239000000499 gel Substances 0.000 description 8
- 238000010438 heat treatment Methods 0.000 description 8
- 239000002609 medium Substances 0.000 description 8
- 102000004169 proteins and genes Human genes 0.000 description 8
- 108090000623 proteins and genes Proteins 0.000 description 8
- 125000004429 atom Chemical group 0.000 description 7
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 7
- 125000005647 linker group Chemical group 0.000 description 7
- 229910052760 oxygen Inorganic materials 0.000 description 7
- 239000001301 oxygen Substances 0.000 description 7
- 230000008569 process Effects 0.000 description 7
- 235000018102 proteins Nutrition 0.000 description 7
- 238000001179 sorption measurement Methods 0.000 description 7
- -1 sulfopropyl group Chemical group 0.000 description 7
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 6
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 6
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 6
- 238000005571 anion exchange chromatography Methods 0.000 description 6
- 239000008367 deionised water Substances 0.000 description 6
- 229910021641 deionized water Inorganic materials 0.000 description 6
- 229920000642 polymer Polymers 0.000 description 6
- 229920002271 DEAE-Sepharose Polymers 0.000 description 5
- PPBRXRYQALVLMV-UHFFFAOYSA-N Styrene Chemical compound C=CC1=CC=CC=C1 PPBRXRYQALVLMV-UHFFFAOYSA-N 0.000 description 5
- 238000004458 analytical method Methods 0.000 description 5
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- 239000000047 product Substances 0.000 description 5
- 238000000926 separation method Methods 0.000 description 5
- 238000000108 ultra-filtration Methods 0.000 description 5
- BFSVOASYOCHEOV-UHFFFAOYSA-N 2-diethylaminoethanol Chemical compound CCN(CC)CCO BFSVOASYOCHEOV-UHFFFAOYSA-N 0.000 description 4
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 4
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 4
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 4
- QAOWNCQODCNURD-UHFFFAOYSA-N Sulfuric acid Chemical compound OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 4
- 238000004587 chromatography analysis Methods 0.000 description 4
- 229940116441 divinylbenzene Drugs 0.000 description 4
- 229910010272 inorganic material Inorganic materials 0.000 description 4
- 239000011147 inorganic material Substances 0.000 description 4
- 150000002500 ions Chemical class 0.000 description 4
- 239000011368 organic material Substances 0.000 description 4
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 4
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 3
- 229920002307 Dextran Polymers 0.000 description 3
- NINIDFKCEFEMDL-UHFFFAOYSA-N Sulfur Chemical compound [S] NINIDFKCEFEMDL-UHFFFAOYSA-N 0.000 description 3
- 229910000147 aluminium phosphate Inorganic materials 0.000 description 3
- 125000003118 aryl group Chemical group 0.000 description 3
- 125000000484 butyl group Chemical group [H]C([*])([H])C([H])([H])C([H])([H])C([H])([H])[H] 0.000 description 3
- 150000001875 compounds Chemical class 0.000 description 3
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- 239000011780 sodium chloride Substances 0.000 description 3
- 229910052717 sulfur Inorganic materials 0.000 description 3
- 239000011593 sulfur Substances 0.000 description 3
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 2
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 2
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 2
- KFZMGEQAYNKOFK-UHFFFAOYSA-N Isopropanol Chemical compound CC(C)O KFZMGEQAYNKOFK-UHFFFAOYSA-N 0.000 description 2
- 241000235058 Komagataella pastoris Species 0.000 description 2
- ABLZXFCXXLZCGV-UHFFFAOYSA-N Phosphorous acid Chemical compound OP(O)=O ABLZXFCXXLZCGV-UHFFFAOYSA-N 0.000 description 2
- BQCADISMDOOEFD-UHFFFAOYSA-N Silver Chemical compound [Ag] BQCADISMDOOEFD-UHFFFAOYSA-N 0.000 description 2
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 2
- 229920002472 Starch Polymers 0.000 description 2
- 229940098773 bovine serum albumin Drugs 0.000 description 2
- 150000001732 carboxylic acid derivatives Chemical class 0.000 description 2
- 229920002678 cellulose Polymers 0.000 description 2
- 239000001913 cellulose Substances 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 239000012504 chromatography matrix 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
- 229920001577 copolymer Polymers 0.000 description 2
- 230000008878 coupling Effects 0.000 description 2
- 238000010168 coupling process Methods 0.000 description 2
- 238000005859 coupling reaction Methods 0.000 description 2
- 238000004132 cross linking Methods 0.000 description 2
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 2
- 235000018417 cysteine Nutrition 0.000 description 2
- 239000000975 dye Substances 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 238000000855 fermentation Methods 0.000 description 2
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- 125000001153 fluoro group Chemical group F* 0.000 description 2
- 229920001600 hydrophobic polymer Polymers 0.000 description 2
- 239000000178 monomer Substances 0.000 description 2
- 238000001426 native polyacrylamide gel electrophoresis Methods 0.000 description 2
- WWZKQHOCKIZLMA-UHFFFAOYSA-N octanoic acid Chemical compound CCCCCCCC(O)=O WWZKQHOCKIZLMA-UHFFFAOYSA-N 0.000 description 2
- 239000002245 particle Substances 0.000 description 2
- 230000002797 proteolythic effect Effects 0.000 description 2
- 230000008929 regeneration Effects 0.000 description 2
- 238000011069 regeneration method Methods 0.000 description 2
- 150000003335 secondary amines Chemical class 0.000 description 2
- 239000000377 silicon dioxide Substances 0.000 description 2
- 229910052709 silver Inorganic materials 0.000 description 2
- 239000004332 silver Substances 0.000 description 2
- 239000001632 sodium acetate Substances 0.000 description 2
- 235000017281 sodium acetate Nutrition 0.000 description 2
- 229960005480 sodium caprylate Drugs 0.000 description 2
- BYKRNSHANADUFY-UHFFFAOYSA-M sodium octanoate Chemical compound [Na+].CCCCCCCC([O-])=O BYKRNSHANADUFY-UHFFFAOYSA-M 0.000 description 2
- 239000003381 stabilizer Substances 0.000 description 2
- 239000008107 starch Substances 0.000 description 2
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- 229920001059 synthetic polymer Polymers 0.000 description 2
- 208000002109 Argyria Diseases 0.000 description 1
- 244000063299 Bacillus subtilis Species 0.000 description 1
- 235000014469 Bacillus subtilis Nutrition 0.000 description 1
- LSNNMFCWUKXFEE-UHFFFAOYSA-M Bisulfite Chemical compound OS([O-])=O LSNNMFCWUKXFEE-UHFFFAOYSA-M 0.000 description 1
- 238000009010 Bradford assay Methods 0.000 description 1
- CURLTUGMZLYLDI-UHFFFAOYSA-N Carbon dioxide Chemical compound O=C=O CURLTUGMZLYLDI-UHFFFAOYSA-N 0.000 description 1
- ZAFNJMIOTHYJRJ-UHFFFAOYSA-N Diisopropyl ether Chemical group CC(C)OC(C)C ZAFNJMIOTHYJRJ-UHFFFAOYSA-N 0.000 description 1
- 241000588724 Escherichia coli Species 0.000 description 1
- 108010024636 Glutathione Proteins 0.000 description 1
- 208000032456 Hemorrhagic Shock Diseases 0.000 description 1
- 241000725303 Human immunodeficiency virus Species 0.000 description 1
- UFHFLCQGNIYNRP-UHFFFAOYSA-N Hydrogen Chemical compound [H][H] UFHFLCQGNIYNRP-UHFFFAOYSA-N 0.000 description 1
- 208000003623 Hypoalbuminemia Diseases 0.000 description 1
- 239000004201 L-cysteine Substances 0.000 description 1
- 235000013878 L-cysteine Nutrition 0.000 description 1
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 241000982698 Prorodonopsis coli Species 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 229920001218 Pullulan Polymers 0.000 description 1
- 239000004373 Pullulan Substances 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 1
- 206010049771 Shock haemorrhagic Diseases 0.000 description 1
- 239000012505 Superdex™ Substances 0.000 description 1
- 102000004142 Trypsin Human genes 0.000 description 1
- 108090000631 Trypsin Proteins 0.000 description 1
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- 238000011481 absorbance measurement Methods 0.000 description 1
- 238000010306 acid treatment Methods 0.000 description 1
- NIXOWILDQLNWCW-UHFFFAOYSA-N acrylic acid group Chemical group C(C=C)(=O)O NIXOWILDQLNWCW-UHFFFAOYSA-N 0.000 description 1
- 230000003044 adaptive effect Effects 0.000 description 1
- 230000000274 adsorptive effect Effects 0.000 description 1
- 229910052783 alkali metal Inorganic materials 0.000 description 1
- 229910052784 alkaline earth metal Inorganic materials 0.000 description 1
- 125000000217 alkyl group Chemical group 0.000 description 1
- OBETXYAYXDNJHR-UHFFFAOYSA-N alpha-ethylcaproic acid Natural products CCCCC(CC)C(O)=O OBETXYAYXDNJHR-UHFFFAOYSA-N 0.000 description 1
- 150000001408 amides Chemical class 0.000 description 1
- 150000003863 ammonium salts Chemical class 0.000 description 1
- 210000004102 animal cell Anatomy 0.000 description 1
- 230000000890 antigenic effect Effects 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
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- 229920001222 biopolymer Polymers 0.000 description 1
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- 210000004369 blood Anatomy 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 230000036770 blood supply Effects 0.000 description 1
- KGBXLFKZBHKPEV-UHFFFAOYSA-N boric acid Chemical compound OB(O)O KGBXLFKZBHKPEV-UHFFFAOYSA-N 0.000 description 1
- 239000004327 boric acid Substances 0.000 description 1
- 125000001246 bromo group Chemical group Br* 0.000 description 1
- 229910052799 carbon Inorganic materials 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- 150000001735 carboxylic acids Chemical class 0.000 description 1
- 125000002091 cationic group Chemical group 0.000 description 1
- 235000010980 cellulose Nutrition 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 150000001793 charged compounds Chemical class 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 125000001309 chloro group Chemical group Cl* 0.000 description 1
- 239000000356 contaminant Substances 0.000 description 1
- 238000011109 contamination Methods 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
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- 239000007857 degradation product Substances 0.000 description 1
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- 125000004185 ester group Chemical group 0.000 description 1
- 150000002148 esters Chemical class 0.000 description 1
- 125000001033 ether group Chemical group 0.000 description 1
- DNJIEGIFACGWOD-UHFFFAOYSA-N ethyl mercaptane Natural products CCS DNJIEGIFACGWOD-UHFFFAOYSA-N 0.000 description 1
- 210000003918 fraction a Anatomy 0.000 description 1
- 239000012520 frozen sample Substances 0.000 description 1
- 238000002523 gelfiltration Methods 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 description 1
- 150000004676 glycans Chemical class 0.000 description 1
- 239000010439 graphite Substances 0.000 description 1
- 229910002804 graphite Inorganic materials 0.000 description 1
- 125000005843 halogen group Chemical group 0.000 description 1
- 208000006454 hepatitis Diseases 0.000 description 1
- 231100000283 hepatitis Toxicity 0.000 description 1
- 125000005842 heteroatom Chemical group 0.000 description 1
- OUUQCZGPVNCOIJ-UHFFFAOYSA-N hydroperoxyl Chemical compound O[O] OUUQCZGPVNCOIJ-UHFFFAOYSA-N 0.000 description 1
- 229920001477 hydrophilic polymer Polymers 0.000 description 1
- 125000001165 hydrophobic group Chemical group 0.000 description 1
- 125000002887 hydroxy group Chemical group [H]O* 0.000 description 1
- 230000003100 immobilizing effect Effects 0.000 description 1
- 125000002346 iodo group Chemical group I* 0.000 description 1
- 238000005342 ion exchange Methods 0.000 description 1
- 238000004255 ion exchange chromatography Methods 0.000 description 1
- 238000004949 mass spectrometry Methods 0.000 description 1
- 238000001840 matrix-assisted laser desorption--ionisation time-of-flight mass spectrometry Methods 0.000 description 1
- 239000002207 metabolite Substances 0.000 description 1
- 150000002734 metacrylic acid derivatives Chemical class 0.000 description 1
- 229910052751 metal Chemical class 0.000 description 1
- 239000002184 metal Chemical class 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 125000004108 n-butyl group Chemical group [H]C([H])([H])C([H])([H])C([H])([H])C([H])([H])* 0.000 description 1
- 229920005615 natural polymer Polymers 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- WWZKQHOCKIZLMA-UHFFFAOYSA-M octanoate Chemical compound CCCCCCCC([O-])=O WWZKQHOCKIZLMA-UHFFFAOYSA-M 0.000 description 1
- 229960002446 octanoic acid Drugs 0.000 description 1
- 125000002347 octyl group Chemical group [H]C([*])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])[H] 0.000 description 1
- 230000003204 osmotic effect Effects 0.000 description 1
- BPUBBGLMJRNUCC-UHFFFAOYSA-N oxygen(2-);tantalum(5+) Chemical compound [O-2].[O-2].[O-2].[O-2].[O-2].[Ta+5].[Ta+5] BPUBBGLMJRNUCC-UHFFFAOYSA-N 0.000 description 1
- RVTZCBVAJQQJTK-UHFFFAOYSA-N oxygen(2-);zirconium(4+) Chemical compound [O-2].[O-2].[Zr+4] RVTZCBVAJQQJTK-UHFFFAOYSA-N 0.000 description 1
- 238000011107 packed bed chromatography Methods 0.000 description 1
- 238000012856 packing Methods 0.000 description 1
- 238000012510 peptide mapping method Methods 0.000 description 1
- 229920002454 poly(glycidyl methacrylate) polymer Polymers 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
- 230000000379 polymerizing effect Effects 0.000 description 1
- 229920001282 polysaccharide Polymers 0.000 description 1
- 239000005017 polysaccharide Substances 0.000 description 1
- 229920002451 polyvinyl alcohol Polymers 0.000 description 1
- 235000019422 polyvinyl alcohol Nutrition 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 150000003141 primary amines Chemical class 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 108090000765 processed proteins & peptides Proteins 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 238000002731 protein assay Methods 0.000 description 1
- 238000001742 protein purification Methods 0.000 description 1
- 235000019423 pullulan Nutrition 0.000 description 1
- 238000010188 recombinant method Methods 0.000 description 1
- 238000004366 reverse phase liquid chromatography Methods 0.000 description 1
- 238000012552 review Methods 0.000 description 1
- 238000005185 salting out Methods 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- RPACBEVZENYWOL-XFULWGLBSA-M sodium;(2r)-2-[6-(4-chlorophenoxy)hexyl]oxirane-2-carboxylate Chemical compound [Na+].C=1C=C(Cl)C=CC=1OCCCCCC[C@]1(C(=O)[O-])CO1 RPACBEVZENYWOL-XFULWGLBSA-M 0.000 description 1
- 238000002336 sorption--desorption measurement Methods 0.000 description 1
- 125000006850 spacer group Chemical group 0.000 description 1
- 229940124530 sulfonamide Drugs 0.000 description 1
- 150000003456 sulfonamides Chemical class 0.000 description 1
- 150000003457 sulfones Chemical class 0.000 description 1
- 150000003462 sulfoxides Chemical class 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 229910001936 tantalum oxide Inorganic materials 0.000 description 1
- 150000003568 thioethers Chemical class 0.000 description 1
- 239000012588 trypsin Substances 0.000 description 1
- 229920003169 water-soluble polymer Polymers 0.000 description 1
- 210000005253 yeast cell Anatomy 0.000 description 1
- 229910001928 zirconium oxide Inorganic materials 0.000 description 1
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 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
- C07K14/76—Albumins
- C07K14/765—Serum albumin, e.g. HSA
-
- 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)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Biophysics (AREA)
- Toxicology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- Genetics & Genomics (AREA)
- Biochemistry (AREA)
- Gastroenterology & Hepatology (AREA)
- Zoology (AREA)
- Animal Behavior & Ethology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Veterinary Medicine (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Chemical & Material Sciences (AREA)
- Diabetes (AREA)
- Pharmacology & Pharmacy (AREA)
- Engineering & Computer Science (AREA)
- Hematology (AREA)
- Public Health (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Treatment Of Liquids With Adsorbents In General (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Solid-Sorbent Or Filter-Aiding Compositions (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| SE0201518A SE526227C2 (sv) | 2002-05-15 | 2002-05-15 | Metod för rening av rekombinant humant serumalbumin |
| PCT/SE2003/000766 WO2003097692A1 (en) | 2002-05-15 | 2003-05-09 | Method for albumin purification |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| JP2006502098A true JP2006502098A (ja) | 2006-01-19 |
Family
ID=20287916
Family Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2004506364A Pending JP2006502098A (ja) | 2002-05-15 | 2003-05-09 | アルブミン精製法 |
| JP2004506365A Expired - Fee Related JP4559216B2 (ja) | 2002-05-15 | 2003-05-15 | 液体中の夾雑物からアルブミンを分離する方法、使用及びキット |
Family Applications After (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
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Families Citing this family (29)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US8802146B2 (en) * | 1998-11-06 | 2014-08-12 | Neomend, Inc. | Systems, methods, and compositions for prevention of tissue adhesion |
| VN23181A1 (en) * | 2003-01-28 | 2010-07-26 | Du Pont | Cyano anthranilamide insecticides |
| WO2004080575A1 (en) * | 2003-03-12 | 2004-09-23 | Fresenius Kabi Deutschland Gmbh | Use of recombinant albumin in dialysis after liver failure |
| CA2564031A1 (en) * | 2004-04-23 | 2005-11-03 | Conjuchem Biotechnologies Inc. | Method for the purification of albumin conjugates |
| CN1854155B (zh) * | 2005-04-29 | 2010-11-17 | 华北制药集团新药研究开发有限责任公司 | 一种纯化rHSA的方法 |
| CL2008002054A1 (es) * | 2007-07-17 | 2009-05-29 | Hoffmann La Roche | Metodo para la regeneracion de una columna de cromatografia de intercambio cationico despues de la elusion de eritropoyetina monopeguilada y metodo para obtener una eritropoyetina monopeguilada, incorporando el metodo de regeneracion de la columna de intercambio cationico. |
| CL2008002053A1 (es) * | 2007-07-17 | 2009-05-22 | Hoffmann La Roche | Metodo para la purificacion de una eritropoyetina monopeguilada (epompeg) que consiste en proporcionar una solucion que contiene eritropoyetina mono, poli y no peguilada y hacerla pasar por dos pasos de cromatografia de intercambio cationico y metodo para producir epo mpeg que incluye metodo de purificacion. |
| CN101978268B (zh) * | 2008-03-31 | 2014-04-23 | 积水医疗株式会社 | 纯化血清白蛋白及免疫学测定方法 |
| US8753868B2 (en) | 2008-08-04 | 2014-06-17 | General Electric Company | Method and system for selective isolation of target biological molecules in a general purpose system |
| CN101768206B (zh) * | 2008-12-31 | 2013-05-15 | 华北制药集团新药研究开发有限责任公司 | 一种重组人血清白蛋白的纯化方法及其应用 |
| WO2010096588A2 (en) | 2009-02-20 | 2010-08-26 | Ventria Bioscience | Cell culture media containing combinations of proteins |
| EP4492053A3 (en) * | 2010-05-25 | 2025-03-19 | F. Hoffmann-La Roche AG | Methods of purifying polypeptides |
| CN102127164B (zh) | 2010-12-20 | 2013-01-30 | 武汉禾元生物科技有限公司 | 一种从水稻种子中提取重组人血清白蛋白的方法 |
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| WO2013134251A2 (en) * | 2012-03-08 | 2013-09-12 | Bio-Rad Laboratories, Inc. | Anionic exchange-hydrophobic mixed mode |
| CN103880947B (zh) | 2012-12-21 | 2016-01-13 | 武汉禾元生物科技股份有限公司 | 一种分离纯化高纯度重组人血清白蛋白的层析方法 |
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| CN107709552B (zh) * | 2015-06-10 | 2022-05-13 | 南克维斯特公司 | 用于治疗癌症的修饰的nk-92细胞 |
| CN106146631A (zh) * | 2015-12-09 | 2016-11-23 | 烟台大学 | 一种离心技术结合疏水层析介质制备藻红蛋白的方法 |
| CN106117326A (zh) * | 2015-12-09 | 2016-11-16 | 烟台大学 | 一种离心法结合阴离子交换层析介质制备藻红蛋白的方法 |
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| IL291020B2 (en) * | 2019-09-24 | 2025-04-01 | Regeneron Pharma | Systems and methods for use in chromatography and regeneration |
| US11739166B2 (en) | 2020-07-02 | 2023-08-29 | Davol Inc. | Reactive polysaccharide-based hemostatic agent |
| US12161777B2 (en) | 2020-07-02 | 2024-12-10 | Davol Inc. | Flowable hemostatic suspension |
| JP7674630B2 (ja) | 2020-12-08 | 2025-05-12 | 通化安睿特生物製薬股▲フェン▼有限公司 | 組換えタンパク質を精製する方法 |
| CN116744984A (zh) | 2020-12-28 | 2023-09-12 | 达沃有限公司 | 包含蛋白质和多官能化改性的基于聚乙二醇的交联剂的反应性干粉状止血材料 |
| CN113461804A (zh) * | 2021-08-09 | 2021-10-01 | 山东健通生物科技有限公司 | 减少重组人血白蛋白发酵过程中色素的方法 |
| CN113880908B (zh) * | 2021-08-25 | 2024-05-14 | 北京伟德杰生物科技有限公司 | 纯化重组人血清白蛋白的融合蛋白的方法 |
| CN113735962B (zh) * | 2021-08-27 | 2023-11-10 | 常熟纳微生物科技有限公司 | 一种从猪血中纯化重组人血清白蛋白的方法及应用 |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH08116985A (ja) * | 1994-08-31 | 1996-05-14 | Green Cross Corp:The | 遺伝子操作に由来するヒト血清アルブミンの精製方法 |
| WO2002005959A2 (en) * | 2000-07-17 | 2002-01-24 | Amersham Biosciences Ab | Adsorption method and ligands |
Family Cites Families (12)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4093612A (en) * | 1975-08-04 | 1978-06-06 | Research Corporation | Selective removal of albumin from blood fluids and compositions therefore |
| FR2403098A1 (fr) * | 1977-09-19 | 1979-04-13 | Merieux Inst | Nouveau materiau capable de fixer de facon reversible des macromolecules biologiques, sa preparation et son application |
| JPH06501033A (ja) * | 1991-07-12 | 1994-01-27 | ギスト ブロカデス ナムローゼ フェンノートシャップ | 血清アルブミンの精製方法 |
| US5849874A (en) * | 1991-07-12 | 1998-12-15 | Gist-Brocades, N.V. | Process for the purification of serum albumin |
| JPH07102148B2 (ja) * | 1992-05-20 | 1995-11-08 | 株式会社ミドリ十字 | 遺伝子操作により得られるヒト血清アルブミンの製造方法、およびそれにより得られるヒト血清アルブミン含有組成物 |
| US5440018A (en) * | 1992-05-20 | 1995-08-08 | The Green Cross Corporation | Recombinant human serum albumin, process for producing the same and pharmaceutical preparation containing the same |
| US5521287A (en) * | 1992-05-20 | 1996-05-28 | The Green Cross Corporation | Recombinant human serum albumin, process for producing the same and pharmaceutical preparation containing the same |
| CA2116385A1 (en) | 1993-02-25 | 1994-08-26 | Akinori Sumi | Human serum albumin and process for producing the same |
| DE69434126T3 (de) * | 1993-12-17 | 2009-07-09 | Mitsubishi Pharma Corp. | Verfahren zum Entfärben von menschlichemn Serum-Albumin |
| CA2157219C (en) * | 1994-08-31 | 2010-10-05 | Munehiro Noda | Process for purifying recombinant human serum albumin |
| GB9902000D0 (en) * | 1999-01-30 | 1999-03-17 | Delta Biotechnology Ltd | Process |
| JP4798832B2 (ja) * | 2000-10-24 | 2011-10-19 | 一般財団法人化学及血清療法研究所 | ヒト血清アルブミン多量体の除去方法 |
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Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH08116985A (ja) * | 1994-08-31 | 1996-05-14 | Green Cross Corp:The | 遺伝子操作に由来するヒト血清アルブミンの精製方法 |
| WO2002005959A2 (en) * | 2000-07-17 | 2002-01-24 | Amersham Biosciences Ab | Adsorption method and ligands |
Also Published As
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| DE60307262D1 (de) | 2006-09-14 |
| AU2003228193A1 (en) | 2003-12-02 |
| ATE335006T1 (de) | 2006-08-15 |
| JP2006512283A (ja) | 2006-04-13 |
| US7351801B2 (en) | 2008-04-01 |
| EP1504032A1 (en) | 2005-02-09 |
| SE0201518D0 (sv) | 2002-05-15 |
| WO2003097693A1 (en) | 2003-11-27 |
| JP4559216B2 (ja) | 2010-10-06 |
| EP1504031A1 (en) | 2005-02-09 |
| US20050215765A1 (en) | 2005-09-29 |
| SE526227C2 (sv) | 2005-08-02 |
| EP1504031B1 (en) | 2006-08-02 |
| US7423124B2 (en) | 2008-09-09 |
| CA2483616A1 (en) | 2003-11-27 |
| CA2483612A1 (en) | 2003-11-27 |
| AU2003232704A1 (en) | 2003-12-02 |
| BRPI0309992B1 (pt) | 2020-12-22 |
| BRPI0309992B8 (pt) | 2023-03-21 |
| AU2003228193B2 (en) | 2009-05-07 |
| ES2268362T3 (es) | 2007-03-16 |
| DE60307262T2 (de) | 2007-06-28 |
| BR0309992A (pt) | 2005-03-01 |
| CN100463921C (zh) | 2009-02-25 |
| IL164844A (en) | 2009-09-01 |
| IL164844A0 (en) | 2005-12-18 |
| US20050214902A1 (en) | 2005-09-29 |
| WO2003097692A1 (en) | 2003-11-27 |
| CN1496993A (zh) | 2004-05-19 |
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