SE526227C2 - Metod för rening av rekombinant humant serumalbumin - Google Patents
Metod för rening av rekombinant humant serumalbuminInfo
- Publication number
- SE526227C2 SE526227C2 SE0201518A SE0201518A SE526227C2 SE 526227 C2 SE526227 C2 SE 526227C2 SE 0201518 A SE0201518 A SE 0201518A SE 0201518 A SE0201518 A SE 0201518A SE 526227 C2 SE526227 C2 SE 526227C2
- Authority
- SE
- Sweden
- Prior art keywords
- matrix
- rhsa
- cation exchange
- ccs
- hic
- Prior art date
Links
- 238000000034 method Methods 0.000 title claims abstract description 59
- 108091006905 Human Serum Albumin Proteins 0.000 title claims abstract description 5
- 102000008100 Human Serum Albumin Human genes 0.000 title claims abstract description 5
- 239000011159 matrix material Substances 0.000 claims abstract description 62
- 238000004191 hydrophobic interaction chromatography Methods 0.000 claims abstract description 30
- 150000003839 salts Chemical class 0.000 claims abstract description 24
- 238000005341 cation exchange Methods 0.000 claims abstract description 22
- 230000002902 bimodal effect Effects 0.000 claims abstract description 12
- 239000012228 culture supernatant Substances 0.000 claims abstract description 11
- 238000004113 cell culture Methods 0.000 claims abstract description 10
- 238000005349 anion exchange Methods 0.000 claims abstract description 7
- 239000003446 ligand Substances 0.000 claims description 44
- 230000003993 interaction Effects 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
- 150000001450 anions Chemical class 0.000 claims description 10
- 238000010438 heat treatment Methods 0.000 claims description 10
- 229910052739 hydrogen Inorganic materials 0.000 claims description 9
- 230000002209 hydrophobic effect Effects 0.000 claims description 9
- 239000001257 hydrogen Substances 0.000 claims description 8
- 238000011210 chromatographic step Methods 0.000 claims description 6
- 239000003638 chemical reducing agent Substances 0.000 claims description 3
- 125000001931 aliphatic group Chemical group 0.000 claims 1
- 125000000623 heterocyclic group Chemical group 0.000 claims 1
- 150000001768 cations Chemical class 0.000 abstract description 25
- 239000000243 solution Substances 0.000 abstract description 12
- 238000000746 purification Methods 0.000 abstract description 11
- 238000010790 dilution Methods 0.000 abstract description 3
- 239000012895 dilution Substances 0.000 abstract description 3
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 16
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 15
- 239000000872 buffer Substances 0.000 description 15
- -1 etc.) Chemical compound 0.000 description 12
- 239000000126 substance Substances 0.000 description 11
- 229920000936 Agarose Polymers 0.000 description 10
- 239000012619 Butyl Sepharose® Substances 0.000 description 9
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 8
- 239000008367 deionised water Substances 0.000 description 8
- 229910021641 deionized water Inorganic materials 0.000 description 8
- 239000000463 material Substances 0.000 description 8
- 125000004429 atom Chemical group 0.000 description 7
- 210000004027 cell Anatomy 0.000 description 7
- 239000000499 gel Substances 0.000 description 7
- 239000002609 medium Substances 0.000 description 7
- 229920000642 polymer Polymers 0.000 description 7
- 235000018102 proteins Nutrition 0.000 description 7
- 102000004169 proteins and genes Human genes 0.000 description 7
- 108090000623 proteins and genes Proteins 0.000 description 7
- 238000001179 sorption measurement Methods 0.000 description 7
- MYRTYDVEIRVNKP-UHFFFAOYSA-N 1,2-Divinylbenzene Chemical class C=CC1=CC=CC=C1C=C MYRTYDVEIRVNKP-UHFFFAOYSA-N 0.000 description 6
- BFSVOASYOCHEOV-UHFFFAOYSA-N 2-diethylaminoethanol Chemical compound CCN(CC)CCO BFSVOASYOCHEOV-UHFFFAOYSA-N 0.000 description 6
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 6
- 230000008901 benefit Effects 0.000 description 6
- 125000000484 butyl group Chemical group [H]C([*])([H])C([H])([H])C([H])([H])C([H])([H])[H] 0.000 description 6
- 238000010828 elution Methods 0.000 description 6
- 125000005647 linker group Chemical group 0.000 description 6
- 238000000926 separation method Methods 0.000 description 6
- 239000002253 acid Substances 0.000 description 5
- 238000005571 anion exchange chromatography Methods 0.000 description 5
- 239000011324 bead Substances 0.000 description 5
- 238000005277 cation exchange chromatography Methods 0.000 description 5
- 238000001962 electrophoresis Methods 0.000 description 5
- 230000008569 process Effects 0.000 description 5
- 230000008929 regeneration Effects 0.000 description 5
- 238000011069 regeneration method Methods 0.000 description 5
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 4
- KFZMGEQAYNKOFK-UHFFFAOYSA-N Isopropanol Chemical compound CC(C)O KFZMGEQAYNKOFK-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
- 229920002684 Sepharose Polymers 0.000 description 4
- PPBRXRYQALVLMV-UHFFFAOYSA-N Styrene Chemical compound C=CC1=CC=CC=C1 PPBRXRYQALVLMV-UHFFFAOYSA-N 0.000 description 4
- 150000001875 compounds Chemical class 0.000 description 4
- 239000012535 impurity Substances 0.000 description 4
- 239000000047 product Substances 0.000 description 4
- 239000011780 sodium chloride Substances 0.000 description 4
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 4
- 238000000108 ultra-filtration Methods 0.000 description 4
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 3
- 208000002109 Argyria Diseases 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
- 125000003118 aryl group Chemical group 0.000 description 3
- 238000000855 fermentation Methods 0.000 description 3
- 230000004151 fermentation Effects 0.000 description 3
- 229910010272 inorganic material Inorganic materials 0.000 description 3
- 239000011147 inorganic material Substances 0.000 description 3
- 150000002500 ions Chemical class 0.000 description 3
- 238000011068 loading method Methods 0.000 description 3
- 238000001426 native polyacrylamide gel electrophoresis Methods 0.000 description 3
- 229910052757 nitrogen Inorganic materials 0.000 description 3
- 239000011368 organic material 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
- 229920002271 DEAE-Sepharose Polymers 0.000 description 2
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 2
- XEEYBQQBJWHFJM-UHFFFAOYSA-N Iron Chemical compound [Fe] XEEYBQQBJWHFJM-UHFFFAOYSA-N 0.000 description 2
- 229910019142 PO4 Inorganic materials 0.000 description 2
- 102000035195 Peptidases Human genes 0.000 description 2
- 108091005804 Peptidases Proteins 0.000 description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-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
- QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 description 2
- MCMNRKCIXSYSNV-UHFFFAOYSA-N Zirconium dioxide Chemical compound O=[Zr]=O MCMNRKCIXSYSNV-UHFFFAOYSA-N 0.000 description 2
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 2
- 229940098773 bovine serum albumin Drugs 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
- 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
- 239000007857 degradation product Substances 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 239000012467 final product Substances 0.000 description 2
- 229920001600 hydrophobic polymer Polymers 0.000 description 2
- 238000005342 ion exchange Methods 0.000 description 2
- 239000000178 monomer Substances 0.000 description 2
- 229910052760 oxygen Inorganic materials 0.000 description 2
- 239000001301 oxygen Substances 0.000 description 2
- 239000002245 particle Substances 0.000 description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 2
- 239000010452 phosphate Substances 0.000 description 2
- 239000000049 pigment Substances 0.000 description 2
- 239000010703 silicon Substances 0.000 description 2
- 229910052710 silicon Inorganic materials 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
- 238000010186 staining Methods 0.000 description 2
- 239000008107 starch Substances 0.000 description 2
- 235000019698 starch Nutrition 0.000 description 2
- 229920001059 synthetic polymer Polymers 0.000 description 2
- 238000011282 treatment Methods 0.000 description 2
- VZEZONWRBFJJMZ-UHFFFAOYSA-N 3-allyl-2-[2-(diethylamino)ethoxy]benzaldehyde Chemical compound CCN(CC)CCOC1=C(CC=C)C=CC=C1C=O VZEZONWRBFJJMZ-UHFFFAOYSA-N 0.000 description 1
- QGZKDVFQNNGYKY-UHFFFAOYSA-O Ammonium Chemical class [NH4+] QGZKDVFQNNGYKY-UHFFFAOYSA-O 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
- 101100069818 Caenorhabditis elegans gur-3 gene Proteins 0.000 description 1
- 101100289200 Caenorhabditis elegans lite-1 gene Proteins 0.000 description 1
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 1
- 108010024636 Glutathione Proteins 0.000 description 1
- UFHFLCQGNIYNRP-UHFFFAOYSA-N Hydrogen Chemical compound [H][H] UFHFLCQGNIYNRP-UHFFFAOYSA-N 0.000 description 1
- 241000235058 Komagataella pastoris Species 0.000 description 1
- 239000004201 L-cysteine Substances 0.000 description 1
- 235000013878 L-cysteine Nutrition 0.000 description 1
- DZTHIGRZJZPRDV-LBPRGKRZSA-N N-acetyl-L-tryptophan Chemical compound C1=CC=C2C(C[C@H](NC(=O)C)C(O)=O)=CNC2=C1 DZTHIGRZJZPRDV-LBPRGKRZSA-N 0.000 description 1
- 229910004727 OSO3H Inorganic materials 0.000 description 1
- 229910018828 PO3H2 Inorganic materials 0.000 description 1
- OAICVXFJPJFONN-UHFFFAOYSA-N Phosphorus Chemical compound [P] OAICVXFJPJFONN-UHFFFAOYSA-N 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
- 229910006069 SO3H Inorganic materials 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 1
- XUIMIQQOPSSXEZ-UHFFFAOYSA-N Silicon Chemical compound [Si] XUIMIQQOPSSXEZ-UHFFFAOYSA-N 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- 238000010306 acid treatment Methods 0.000 description 1
- 229910052783 alkali metal Inorganic materials 0.000 description 1
- 150000001340 alkali metals Chemical class 0.000 description 1
- 229910052784 alkaline earth metal Inorganic materials 0.000 description 1
- 150000001342 alkaline earth metals Chemical class 0.000 description 1
- 125000000217 alkyl group Chemical group 0.000 description 1
- 150000001408 amides Chemical class 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 210000004102 animal cell Anatomy 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 239000007853 buffer solution Substances 0.000 description 1
- 125000002915 carbonyl group Chemical group [*:2]C([*:1])=O 0.000 description 1
- 150000007942 carboxylates Chemical class 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
- 238000004587 chromatography analysis Methods 0.000 description 1
- 238000004140 cleaning Methods 0.000 description 1
- 239000013065 commercial product Substances 0.000 description 1
- 239000000356 contaminant Substances 0.000 description 1
- 230000008878 coupling Effects 0.000 description 1
- 238000010168 coupling process Methods 0.000 description 1
- 238000005859 coupling reaction Methods 0.000 description 1
- 238000003795 desorption Methods 0.000 description 1
- 239000003480 eluent Substances 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 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
- 150000002170 ethers Chemical class 0.000 description 1
- DNJIEGIFACGWOD-UHFFFAOYSA-N ethyl mercaptane Natural products CCS DNJIEGIFACGWOD-UHFFFAOYSA-N 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 210000003918 fraction a Anatomy 0.000 description 1
- ZZUFCTLCJUWOSV-UHFFFAOYSA-N furosemide Chemical compound C1=C(Cl)C(S(=O)(=O)N)=CC(C(O)=O)=C1NCC1=CC=CO1 ZZUFCTLCJUWOSV-UHFFFAOYSA-N 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
- 239000001963 growth medium Substances 0.000 description 1
- 125000005843 halogen group Chemical group 0.000 description 1
- 125000005842 heteroatom Chemical group 0.000 description 1
- 230000003301 hydrolyzing effect Effects 0.000 description 1
- 229920001477 hydrophilic polymer Polymers 0.000 description 1
- 125000001165 hydrophobic group Chemical group 0.000 description 1
- 150000001261 hydroxy acids Chemical class 0.000 description 1
- 125000002887 hydroxy group Chemical group [H]O* 0.000 description 1
- 230000003100 immobilizing effect Effects 0.000 description 1
- 229910052742 iron Inorganic materials 0.000 description 1
- 125000001449 isopropyl group Chemical group [H]C([H])([H])C([H])(*)C([H])([H])[H] 0.000 description 1
- 238000002386 leaching Methods 0.000 description 1
- 238000004519 manufacturing process 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
- 238000005259 measurement Methods 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
- WWZKQHOCKIZLMA-UHFFFAOYSA-N octanoic acid Chemical compound CCCCCCCC(O)=O WWZKQHOCKIZLMA-UHFFFAOYSA-N 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
- 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
- 238000012510 peptide mapping method Methods 0.000 description 1
- 229910052698 phosphorus Inorganic materials 0.000 description 1
- 239000011574 phosphorus Substances 0.000 description 1
- 229920002401 polyacrylamide Polymers 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
- 238000002360 preparation method Methods 0.000 description 1
- 238000004321 preservation Methods 0.000 description 1
- 150000003141 primary amines Chemical class 0.000 description 1
- 108090000765 processed proteins & peptides Proteins 0.000 description 1
- 102000004196 processed proteins & peptides Human genes 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 238000002731 protein assay Methods 0.000 description 1
- 230000017854 proteolysis Effects 0.000 description 1
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 1
- 235000019423 pullulan Nutrition 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 238000004366 reverse phase liquid chromatography Methods 0.000 description 1
- 238000005185 salting out Methods 0.000 description 1
- 238000013341 scale-up Methods 0.000 description 1
- 150000003335 secondary amines Chemical class 0.000 description 1
- 159000000000 sodium salts Chemical class 0.000 description 1
- 238000002336 sorption--desorption measurement Methods 0.000 description 1
- 125000006850 spacer group Chemical group 0.000 description 1
- BDHFUVZGWQCTTF-UHFFFAOYSA-M sulfonate Chemical compound [O-]S(=O)=O BDHFUVZGWQCTTF-UHFFFAOYSA-M 0.000 description 1
- 150000003462 sulfoxides Chemical class 0.000 description 1
- 238000004381 surface treatment Methods 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 229910001936 tantalum oxide Inorganic materials 0.000 description 1
- 150000003568 thioethers Chemical class 0.000 description 1
- 210000005253 yeast cell Anatomy 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)
- Biochemistry (AREA)
- Biophysics (AREA)
- Gastroenterology & Hepatology (AREA)
- Genetics & Genomics (AREA)
- Zoology (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Toxicology (AREA)
- Engineering & Computer Science (AREA)
- Public Health (AREA)
- Diabetes (AREA)
- Hematology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Veterinary Medicine (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)
Priority Applications (20)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| SE0201518A SE526227C2 (sv) | 2002-05-15 | 2002-05-15 | Metod för rening av rekombinant humant serumalbumin |
| AU2003228193A AU2003228193B2 (en) | 2002-05-15 | 2003-05-09 | Method for albumin purification |
| JP2004506364A JP2006502098A (ja) | 2002-05-15 | 2003-05-09 | アルブミン精製法 |
| CA002483612A CA2483612A1 (en) | 2002-05-15 | 2003-05-09 | Method for albumin purification |
| US10/514,536 US7423124B2 (en) | 2002-05-15 | 2003-05-09 | Method for albumin purification |
| DE60307262T DE60307262T2 (de) | 2002-05-15 | 2003-05-09 | Verfahren zur aufreinigung von albumin |
| PCT/SE2003/000766 WO2003097692A1 (en) | 2002-05-15 | 2003-05-09 | Method for albumin purification |
| BRPI0309992-0A BRPI0309992B1 (pt) | 2002-05-15 | 2003-05-09 | método para purificar albumina de soro humano recombinante (rhsa) de uma solução |
| BRPI0309992A BRPI0309992B8 (pt) | 2002-05-15 | 2003-05-09 | método para purificar albumina de soro humano recombinante (rhsa) de uma solução |
| ES03725953T ES2268362T3 (es) | 2002-05-15 | 2003-05-09 | Metodo para purificacion de albumina. |
| AT03725953T ATE335006T1 (de) | 2002-05-15 | 2003-05-09 | Verfahren zur aufreinigung von albumin |
| EP03725953A EP1504031B1 (en) | 2002-05-15 | 2003-05-09 | Method for albumin purification |
| CNB031235026A CN100463921C (zh) | 2002-05-15 | 2003-05-09 | 白蛋白纯化 |
| US10/514,544 US7351801B2 (en) | 2002-05-15 | 2003-05-15 | Method, use and kit for separating albumin from contaminants in a liquid |
| PCT/SE2003/000792 WO2003097693A1 (en) | 2002-05-15 | 2003-05-15 | Method, use and kit for separating albumin from contaminants in a liquid |
| JP2004506365A 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 |
| AU2003232704A AU2003232704A1 (en) | 2002-05-15 | 2003-05-15 | Method, use and kit for separating albumin from contaminants in a liquid |
| CA002483616A CA2483616A1 (en) | 2002-05-15 | 2003-05-15 | Method, use and kit for separating albumin from contaminants in a liquid |
| EP03752962A EP1504032A1 (en) | 2002-05-15 | 2003-05-15 | Method, use and kit for separating albumin from contaminants in a liquid |
| IL164844A IL164844A (en) | 2002-05-15 | 2004-10-26 | Method for albumin purification |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| SE0201518A SE526227C2 (sv) | 2002-05-15 | 2002-05-15 | Metod för rening av rekombinant humant serumalbumin |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| SE0201518D0 SE0201518D0 (sv) | 2002-05-15 |
| SE526227C2 true SE526227C2 (sv) | 2005-08-02 |
Family
ID=20287916
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| SE0201518A SE526227C2 (sv) | 2002-05-15 | 2002-05-15 | Metod för rening av rekombinant humant serumalbumin |
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| US (2) | US7423124B2 (https=) |
| EP (2) | EP1504031B1 (https=) |
| JP (2) | JP2006502098A (https=) |
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| AT (1) | ATE335006T1 (https=) |
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| BR (2) | BRPI0309992B1 (https=) |
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| IL (1) | IL164844A (https=) |
| SE (1) | SE526227C2 (https=) |
| WO (2) | WO2003097692A1 (https=) |
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| US8802146B2 (en) * | 1998-11-06 | 2014-08-12 | Neomend, Inc. | Systems, methods, and compositions for prevention of tissue adhesion |
| SI1599463T1 (sl) * | 2003-01-28 | 2013-10-30 | E.I. Du Pont De Nemours And Company | Ciano antranilamidni insekticidi |
| CA2514981A1 (en) * | 2003-03-12 | 2004-09-23 | Fresenius Kabi Deutschland Gmbh | Use of recombinant albumin in dialysis after liver failure |
| DK2100904T3 (da) * | 2004-04-23 | 2010-11-08 | Conjuchem Biotechnologies Inc | Fast fase til anvendelse i en fremgangsmåde til rensning af albuminkonjugater |
| 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 |
| CA2752729A1 (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 |
| CN102532254B (zh) * | 2010-12-24 | 2015-06-24 | 武汉禾元生物科技股份有限公司 | 一种从水稻种子中分离纯化重组人血清白蛋白的方法 |
| CN104812491B (zh) * | 2012-03-08 | 2018-06-19 | 生物辐射实验室股份有限公司 | 阴离子交换-疏水性混合模式 |
| 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 |
| CN103923211A (zh) * | 2014-05-08 | 2014-07-16 | 齐智 | 一种医药级重组人血清白蛋白的纯化方法 |
| EP4424326A3 (en) | 2015-06-10 | 2024-11-13 | ImmunityBio, Inc. | Modified nk-92 cells for treating cancer |
| 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 |
| 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 |
| CN106117347A (zh) * | 2015-12-09 | 2016-11-16 | 烟台大学 | 一种疏水层析制备高纯度藻红蛋白的方法 |
| EP4653865A3 (en) | 2019-09-24 | 2026-02-18 | Regeneron Pharmaceuticals, Inc. | Systems and methods for chromatography use and regeneration |
| US12161777B2 (en) | 2020-07-02 | 2024-12-10 | Davol Inc. | Flowable hemostatic suspension |
| US11739166B2 (en) | 2020-07-02 | 2023-08-29 | Davol Inc. | Reactive polysaccharide-based hemostatic agent |
| WO2022120547A1 (zh) | 2020-12-08 | 2022-06-16 | 通化安睿特生物制药股份有限公司 | 纯化重组蛋白的方法 |
| EP4267210A1 (en) | 2020-12-28 | 2023-11-01 | Davol Inc. | Reactive dry powdered hemostatic materials comprising a protein and a multifunctionalized modified polyethylene glycol based crosslinking agent |
| 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 |
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| 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 |
| US5849874A (en) * | 1991-07-12 | 1998-12-15 | Gist-Brocades, N.V. | Process for the purification of serum albumin |
| DE69230273T2 (de) * | 1991-07-12 | 2000-05-31 | Dsm N.V., Heerlen | Verfahren zur Reinigung von Serumalbumin |
| 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 |
| 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 |
| 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 |
| CA2116385A1 (en) * | 1993-02-25 | 1994-08-26 | Akinori Sumi | Human serum albumin and process for producing the same |
| CA2138349A1 (en) * | 1993-12-17 | 1995-06-18 | Welfide Corporation | Method for decoloring human serum albumin |
| CA2157219C (en) | 1994-08-31 | 2010-10-05 | Munehiro Noda | Process for purifying recombinant human serum albumin |
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| GB9902000D0 (en) * | 1999-01-30 | 1999-03-17 | Delta Biotechnology Ltd | Process |
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| 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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2002
- 2002-05-15 SE SE0201518A patent/SE526227C2/sv not_active IP Right Cessation
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2003
- 2003-05-09 US US10/514,536 patent/US7423124B2/en not_active Expired - Lifetime
- 2003-05-09 ES ES03725953T patent/ES2268362T3/es not_active Expired - Lifetime
- 2003-05-09 BR BRPI0309992-0A patent/BRPI0309992B1/pt active IP Right Grant
- 2003-05-09 EP EP03725953A patent/EP1504031B1/en not_active Expired - Lifetime
- 2003-05-09 WO PCT/SE2003/000766 patent/WO2003097692A1/en not_active Ceased
- 2003-05-09 JP JP2004506364A patent/JP2006502098A/ja active Pending
- 2003-05-09 CN CNB031235026A patent/CN100463921C/zh not_active Expired - Fee Related
- 2003-05-09 BR BRPI0309992A patent/BRPI0309992B8/pt active IP Right Grant
- 2003-05-09 CA CA002483612A patent/CA2483612A1/en not_active Abandoned
- 2003-05-09 AT AT03725953T patent/ATE335006T1/de not_active IP Right Cessation
- 2003-05-09 DE DE60307262T patent/DE60307262T2/de not_active Expired - Lifetime
- 2003-05-09 AU AU2003228193A patent/AU2003228193B2/en not_active Ceased
- 2003-05-15 AU AU2003232704A patent/AU2003232704A1/en not_active Abandoned
- 2003-05-15 CA CA002483616A patent/CA2483616A1/en not_active Abandoned
- 2003-05-15 EP EP03752962A patent/EP1504032A1/en not_active Withdrawn
- 2003-05-15 US US10/514,544 patent/US7351801B2/en not_active Expired - Fee Related
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Also Published As
| Publication number | Publication date |
|---|---|
| BRPI0309992B8 (pt) | 2023-03-21 |
| AU2003228193A1 (en) | 2003-12-02 |
| EP1504032A1 (en) | 2005-02-09 |
| ATE335006T1 (de) | 2006-08-15 |
| DE60307262D1 (de) | 2006-09-14 |
| SE0201518D0 (sv) | 2002-05-15 |
| JP4559216B2 (ja) | 2010-10-06 |
| JP2006502098A (ja) | 2006-01-19 |
| US20050214902A1 (en) | 2005-09-29 |
| WO2003097693A1 (en) | 2003-11-27 |
| BRPI0309992B1 (pt) | 2020-12-22 |
| ES2268362T3 (es) | 2007-03-16 |
| CA2483616A1 (en) | 2003-11-27 |
| BR0309992A (pt) | 2005-03-01 |
| AU2003228193B2 (en) | 2009-05-07 |
| JP2006512283A (ja) | 2006-04-13 |
| US7423124B2 (en) | 2008-09-09 |
| US7351801B2 (en) | 2008-04-01 |
| CN100463921C (zh) | 2009-02-25 |
| DE60307262T2 (de) | 2007-06-28 |
| IL164844A (en) | 2009-09-01 |
| IL164844A0 (en) | 2005-12-18 |
| WO2003097692A1 (en) | 2003-11-27 |
| EP1504031B1 (en) | 2006-08-02 |
| US20050215765A1 (en) | 2005-09-29 |
| AU2003232704A1 (en) | 2003-12-02 |
| EP1504031A1 (en) | 2005-02-09 |
| CA2483612A1 (en) | 2003-11-27 |
| CN1496993A (zh) | 2004-05-19 |
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