LT3417B - Blood coagulation factor xi concentrate and process for the preparing same - Google Patents
Blood coagulation factor xi concentrate and process for the preparing same Download PDFInfo
- Publication number
- LT3417B LT3417B LTIP265A LTIP265A LT3417B LT 3417 B LT3417 B LT 3417B LT IP265 A LTIP265 A LT IP265A LT IP265 A LTIP265 A LT IP265A LT 3417 B LT3417 B LT 3417B
- Authority
- LT
- Lithuania
- Prior art keywords
- factor
- filter
- concentrate
- sodium chloride
- buffer
- Prior art date
Links
- 108010074864 Factor XI Proteins 0.000 title claims abstract description 56
- 238000000034 method Methods 0.000 title claims abstract description 27
- 239000012141 concentrate Substances 0.000 title claims abstract description 15
- 230000000694 effects Effects 0.000 claims abstract description 14
- 230000001225 therapeutic effect Effects 0.000 claims abstract description 8
- 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 claims abstract description 5
- 239000003729 cation exchange resin Substances 0.000 claims abstract description 5
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 claims description 33
- 239000011780 sodium chloride Substances 0.000 claims description 17
- 102000004169 proteins and genes Human genes 0.000 claims description 15
- 108090000623 proteins and genes Proteins 0.000 claims description 15
- 239000000872 buffer Substances 0.000 claims description 14
- LWIHDJKSTIGBAC-UHFFFAOYSA-K tripotassium phosphate Chemical compound [K+].[K+].[K+].[O-]P([O-])([O-])=O LWIHDJKSTIGBAC-UHFFFAOYSA-K 0.000 claims description 14
- 235000002639 sodium chloride Nutrition 0.000 claims description 13
- 239000001509 sodium citrate Substances 0.000 claims description 10
- NLJMYIDDQXHKNR-UHFFFAOYSA-K sodium citrate Chemical compound O.O.[Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O NLJMYIDDQXHKNR-UHFFFAOYSA-K 0.000 claims description 10
- 239000006228 supernatant Substances 0.000 claims description 9
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 claims description 7
- 229920002684 Sepharose Polymers 0.000 claims description 7
- BNIILDVGGAEEIG-UHFFFAOYSA-L disodium hydrogen phosphate Chemical compound [Na+].[Na+].OP([O-])([O-])=O BNIILDVGGAEEIG-UHFFFAOYSA-L 0.000 claims description 7
- 229910000397 disodium phosphate Inorganic materials 0.000 claims description 7
- 235000019800 disodium phosphate Nutrition 0.000 claims description 7
- 229910000160 potassium phosphate Inorganic materials 0.000 claims description 7
- 235000011009 potassium phosphates Nutrition 0.000 claims description 7
- 239000001488 sodium phosphate Substances 0.000 claims description 7
- 239000004472 Lysine Substances 0.000 claims description 6
- 239000004475 Arginine Substances 0.000 claims description 5
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 claims description 5
- QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 claims description 5
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 claims description 5
- 235000011083 sodium citrates Nutrition 0.000 claims description 5
- 102000004411 Antithrombin III Human genes 0.000 claims description 4
- 108090000935 Antithrombin III Proteins 0.000 claims description 4
- HTTJABKRGRZYRN-UHFFFAOYSA-N Heparin Chemical compound OC1C(NC(=O)C)C(O)OC(COS(O)(=O)=O)C1OC1C(OS(O)(=O)=O)C(O)C(OC2C(C(OS(O)(=O)=O)C(OC3C(C(O)C(O)C(O3)C(O)=O)OS(O)(=O)=O)C(CO)O2)NS(O)(=O)=O)C(C(O)=O)O1 HTTJABKRGRZYRN-UHFFFAOYSA-N 0.000 claims description 4
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 claims description 4
- 229960005348 antithrombin iii Drugs 0.000 claims description 4
- 229960002897 heparin Drugs 0.000 claims description 4
- 229920000669 heparin Polymers 0.000 claims description 4
- 238000000502 dialysis Methods 0.000 claims description 3
- 238000005406 washing Methods 0.000 claims description 3
- 239000001913 cellulose Substances 0.000 claims description 2
- 229920002678 cellulose Polymers 0.000 claims description 2
- 238000011068 loading method Methods 0.000 claims description 2
- 239000011148 porous material Substances 0.000 claims description 2
- QXNVGIXVLWOKEQ-UHFFFAOYSA-N Disodium Chemical class [Na][Na] QXNVGIXVLWOKEQ-UHFFFAOYSA-N 0.000 claims 1
- ZGTMUACCHSMWAC-UHFFFAOYSA-L EDTA disodium salt (anhydrous) Chemical compound [Na+].[Na+].OC(=O)CN(CC([O-])=O)CCN(CC(O)=O)CC([O-])=O ZGTMUACCHSMWAC-UHFFFAOYSA-L 0.000 claims 1
- 230000000840 anti-viral effect Effects 0.000 claims 1
- 150000001768 cations Chemical class 0.000 claims 1
- 238000003795 desorption Methods 0.000 claims 1
- 238000001179 sorption measurement Methods 0.000 abstract description 6
- 238000004587 chromatography analysis Methods 0.000 abstract description 5
- 201000007219 factor XI deficiency Diseases 0.000 abstract description 3
- 238000009256 replacement therapy Methods 0.000 abstract description 2
- 235000018102 proteins Nutrition 0.000 description 13
- 238000000746 purification Methods 0.000 description 10
- 238000002360 preparation method Methods 0.000 description 9
- 238000010828 elution Methods 0.000 description 6
- 238000001914 filtration Methods 0.000 description 6
- 239000000243 solution Substances 0.000 description 5
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 4
- 108010017384 Blood Proteins Proteins 0.000 description 3
- 102000004506 Blood Proteins Human genes 0.000 description 3
- 241000700605 Viruses Species 0.000 description 3
- 235000009697 arginine Nutrition 0.000 description 3
- 230000023555 blood coagulation Effects 0.000 description 3
- 239000007853 buffer solution Substances 0.000 description 3
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 description 3
- 238000004140 cleaning Methods 0.000 description 3
- 239000003599 detergent Substances 0.000 description 3
- 238000010790 dilution Methods 0.000 description 3
- 239000012895 dilution Substances 0.000 description 3
- 230000002779 inactivation Effects 0.000 description 3
- 235000018977 lysine Nutrition 0.000 description 3
- 239000000047 product Substances 0.000 description 3
- 239000011347 resin Substances 0.000 description 3
- 229920005989 resin Polymers 0.000 description 3
- 230000003612 virological effect Effects 0.000 description 3
- 239000011534 wash buffer Substances 0.000 description 3
- 102100022641 Coagulation factor IX Human genes 0.000 description 2
- 239000003109 Disodium ethylene diamine tetraacetate Substances 0.000 description 2
- 108010076282 Factor IX Proteins 0.000 description 2
- 102000016359 Fibronectins Human genes 0.000 description 2
- 108010067306 Fibronectins Proteins 0.000 description 2
- 208000001953 Hypotension Diseases 0.000 description 2
- 241001465754 Metazoa Species 0.000 description 2
- 241000699670 Mus sp. Species 0.000 description 2
- 241000283973 Oryctolagus cuniculus Species 0.000 description 2
- 102000035195 Peptidases Human genes 0.000 description 2
- 108091005804 Peptidases Proteins 0.000 description 2
- 239000004365 Protease Substances 0.000 description 2
- 241000700159 Rattus Species 0.000 description 2
- 230000003213 activating effect Effects 0.000 description 2
- 238000004166 bioassay Methods 0.000 description 2
- 238000010256 biochemical assay Methods 0.000 description 2
- 239000003795 chemical substances by application Substances 0.000 description 2
- 239000000356 contaminant Substances 0.000 description 2
- 235000019301 disodium ethylene diamine tetraacetate Nutrition 0.000 description 2
- 238000001962 electrophoresis Methods 0.000 description 2
- 229960004222 factor ix Drugs 0.000 description 2
- 230000036543 hypotension Effects 0.000 description 2
- 230000000415 inactivating effect Effects 0.000 description 2
- 239000003112 inhibitor Substances 0.000 description 2
- 238000002347 injection Methods 0.000 description 2
- 239000007924 injection Substances 0.000 description 2
- 229920002401 polyacrylamide Polymers 0.000 description 2
- 239000007858 starting material Substances 0.000 description 2
- 238000002560 therapeutic procedure Methods 0.000 description 2
- 230000002885 thrombogenetic effect Effects 0.000 description 2
- STCOOQWBFONSKY-UHFFFAOYSA-N tributyl phosphate Chemical compound CCCCOP(=O)(OCCCC)OCCCC STCOOQWBFONSKY-UHFFFAOYSA-N 0.000 description 2
- 238000000108 ultra-filtration Methods 0.000 description 2
- PGOHTUIFYSHAQG-LJSDBVFPSA-N (2S)-6-amino-2-[[(2S)-5-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-4-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-5-amino-2-[[(2S)-5-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S,3R)-2-[[(2S)-5-amino-2-[[(2S)-2-[[(2S)-2-[[(2S,3R)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-5-amino-2-[[(2S)-1-[(2S,3R)-2-[[(2S)-2-[[(2S)-2-[[(2R)-2-[[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-1-[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-amino-4-methylsulfanylbutanoyl]amino]-3-(1H-indol-3-yl)propanoyl]amino]-5-carbamimidamidopentanoyl]amino]propanoyl]pyrrolidine-2-carbonyl]amino]-3-methylbutanoyl]amino]-4-methylpentanoyl]amino]-4-methylpentanoyl]amino]acetyl]amino]-3-hydroxypropanoyl]amino]-4-methylpentanoyl]amino]-3-sulfanylpropanoyl]amino]-4-methylsulfanylbutanoyl]amino]-5-carbamimidamidopentanoyl]amino]-3-hydroxybutanoyl]pyrrolidine-2-carbonyl]amino]-5-oxopentanoyl]amino]-3-hydroxypropanoyl]amino]-3-hydroxypropanoyl]amino]-3-(1H-imidazol-5-yl)propanoyl]amino]-4-methylpentanoyl]amino]-3-hydroxybutanoyl]amino]-3-(1H-indol-3-yl)propanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-oxopentanoyl]amino]-3-hydroxybutanoyl]amino]-3-hydroxypropanoyl]amino]-3-carboxypropanoyl]amino]-3-hydroxypropanoyl]amino]-5-oxopentanoyl]amino]-5-oxopentanoyl]amino]-3-phenylpropanoyl]amino]-5-carbamimidamidopentanoyl]amino]-3-methylbutanoyl]amino]-4-methylpentanoyl]amino]-4-oxobutanoyl]amino]-5-carbamimidamidopentanoyl]amino]-3-(1H-indol-3-yl)propanoyl]amino]-4-carboxybutanoyl]amino]-5-oxopentanoyl]amino]hexanoic acid Chemical compound CSCC[C@H](N)C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C)C(=O)N1CCC[C@H]1C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)N[C@@H](Cc1cnc[nH]1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCCCN)C(O)=O PGOHTUIFYSHAQG-LJSDBVFPSA-N 0.000 description 1
- GHCZTIFQWKKGSB-UHFFFAOYSA-N 2-hydroxypropane-1,2,3-tricarboxylic acid;phosphoric acid Chemical compound OP(O)(O)=O.OC(=O)CC(O)(C(O)=O)CC(O)=O GHCZTIFQWKKGSB-UHFFFAOYSA-N 0.000 description 1
- 208000024178 Acquired factor XI deficiency Diseases 0.000 description 1
- 102100033312 Alpha-2-macroglobulin Human genes 0.000 description 1
- 108010039209 Blood Coagulation Factors Proteins 0.000 description 1
- 102000015081 Blood Coagulation Factors Human genes 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 241000252095 Congridae Species 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 108010014173 Factor X Proteins 0.000 description 1
- 108010071289 Factor XIII Proteins 0.000 description 1
- 102000003886 Glycoproteins Human genes 0.000 description 1
- 108090000288 Glycoproteins Proteins 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 102000002397 Kinins Human genes 0.000 description 1
- 108010093008 Kinins Proteins 0.000 description 1
- 235000019766 L-Lysine Nutrition 0.000 description 1
- ODKSFYDXXFIFQN-BYPYZUCNSA-N L-arginine Chemical compound OC(=O)[C@@H](N)CCCN=C(N)N ODKSFYDXXFIFQN-BYPYZUCNSA-N 0.000 description 1
- 229930064664 L-arginine Natural products 0.000 description 1
- 235000014852 L-arginine Nutrition 0.000 description 1
- 229920001410 Microfiber Polymers 0.000 description 1
- 108010051456 Plasminogen Proteins 0.000 description 1
- 102100038124 Plasminogen Human genes 0.000 description 1
- 108010015078 Pregnancy-Associated alpha 2-Macroglobulins Proteins 0.000 description 1
- 108010000499 Thromboplastin Proteins 0.000 description 1
- 102000002262 Thromboplastin Human genes 0.000 description 1
- 208000007536 Thrombosis Diseases 0.000 description 1
- 239000003463 adsorbent Substances 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 238000010171 animal model Methods 0.000 description 1
- 239000010425 asbestos Substances 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 239000003114 blood coagulation factor Substances 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 238000011210 chromatographic step Methods 0.000 description 1
- 230000015271 coagulation Effects 0.000 description 1
- 238000005345 coagulation Methods 0.000 description 1
- 208000011664 congenital factor XI deficiency Diseases 0.000 description 1
- 238000011109 contamination Methods 0.000 description 1
- 238000005202 decontamination Methods 0.000 description 1
- 230000003588 decontaminative effect Effects 0.000 description 1
- 239000012149 elution buffer Substances 0.000 description 1
- 229940088598 enzyme Drugs 0.000 description 1
- 229940012444 factor xiii Drugs 0.000 description 1
- 239000003527 fibrinolytic agent Substances 0.000 description 1
- 230000003480 fibrinolytic effect Effects 0.000 description 1
- 239000000706 filtrate Substances 0.000 description 1
- 238000011010 flushing procedure Methods 0.000 description 1
- 238000004108 freeze drying Methods 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- 230000023597 hemostasis Effects 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 238000001990 intravenous administration Methods 0.000 description 1
- 238000004255 ion exchange chromatography Methods 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 238000011031 large-scale manufacturing process Methods 0.000 description 1
- 231100000518 lethal Toxicity 0.000 description 1
- 230000001665 lethal effect Effects 0.000 description 1
- 239000012931 lyophilized formulation Substances 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 210000004779 membrane envelope Anatomy 0.000 description 1
- 239000003658 microfiber Substances 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 238000006386 neutralization reaction Methods 0.000 description 1
- 229910001562 pearlite Inorganic materials 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 229920000136 polysorbate Polymers 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 230000001681 protective effect Effects 0.000 description 1
- 239000012460 protein solution Substances 0.000 description 1
- 108010012557 prothrombin complex concentrates Proteins 0.000 description 1
- 239000012264 purified product Substances 0.000 description 1
- 230000001105 regulatory effect Effects 0.000 description 1
- 229910052895 riebeckite Inorganic materials 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 238000010572 single replacement reaction Methods 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 241000894007 species Species 0.000 description 1
- -1 sulfopropyl groups Chemical group 0.000 description 1
- 229910021653 sulphate ion Inorganic materials 0.000 description 1
- 238000010257 thawing Methods 0.000 description 1
- 231100000820 toxicity test Toxicity 0.000 description 1
- 230000002227 vasoactive effect Effects 0.000 description 1
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/64—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue
- C12N9/6421—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
- C12N9/6424—Serine endopeptidases (3.4.21)
- C12N9/6443—Coagulation factor XIa (3.4.21.27)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y304/00—Hydrolases acting on peptide bonds, i.e. peptidases (3.4)
- C12Y304/21—Serine endopeptidases (3.4.21)
- C12Y304/21027—Coagulation factor XIa (3.4.21.27)
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Genetics & Genomics (AREA)
- Wood Science & Technology (AREA)
- Zoology (AREA)
- Biomedical Technology (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- General Engineering & Computer Science (AREA)
- Medicinal Chemistry (AREA)
- Microbiology (AREA)
- Biotechnology (AREA)
- Molecular Biology (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| FR9105572A FR2676231A1 (fr) | 1991-05-07 | 1991-05-07 | Concentre de facteur xi de la coagulation sanguine a haute activite specifique, approprie a usage therapeutique et son procede de preparation. |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| LTIP265A LTIP265A (en) | 1994-10-25 |
| LT3417B true LT3417B (en) | 1995-09-25 |
Family
ID=9412593
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| LTIP265A LT3417B (en) | 1991-05-07 | 1992-12-29 | Blood coagulation factor xi concentrate and process for the preparing same |
Country Status (16)
| Country | Link |
|---|---|
| US (1) | US5252217A (OSRAM) |
| EP (1) | EP0512883B1 (OSRAM) |
| AT (1) | ATE156360T1 (OSRAM) |
| AU (1) | AU652043B2 (OSRAM) |
| BR (1) | BR9201718A (OSRAM) |
| CA (1) | CA2068069C (OSRAM) |
| DE (1) | DE69221369T2 (OSRAM) |
| DK (1) | DK0512883T3 (OSRAM) |
| EE (1) | EE03017B1 (OSRAM) |
| ES (1) | ES2107511T3 (OSRAM) |
| FR (1) | FR2676231A1 (OSRAM) |
| GR (1) | GR3025134T3 (OSRAM) |
| IL (1) | IL99567A (OSRAM) |
| LT (1) | LT3417B (OSRAM) |
| RU (1) | RU2097047C1 (OSRAM) |
| UA (1) | UA27733C2 (OSRAM) |
Families Citing this family (17)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| RU2151604C1 (ru) * | 1999-01-21 | 2000-06-27 | Станкевич Виктор Евгеньевич | Способ приготовления универсальной гемотрансфузионной среды |
| AU2002354846B2 (en) * | 2001-07-20 | 2007-08-02 | Novo Nordisk Health Care Ag | Pharmaceutical composition comprising factor VII polypeptides and factor XI polypeptides |
| US20030040480A1 (en) * | 2001-07-20 | 2003-02-27 | Rasmus Rojkjaer | Pharmaceutical composition comprising factor VII polypeptides and factor XI polypeptides |
| KR20060118486A (ko) * | 2003-11-20 | 2006-11-23 | 노보 노르디스크 헬스 케어 악티엔게젤샤프트 | 인자 ｘｉ의 치료적 사용 |
| US20050181978A1 (en) * | 2003-11-20 | 2005-08-18 | Rasmus Rojkjaer | Therapeutic use of factor XI |
| WO2006128497A1 (en) * | 2005-06-01 | 2006-12-07 | Novo Nordisk A/S | Pharmaceutical formulation of factor xi |
| CL2007002615A1 (es) * | 2006-09-08 | 2008-04-18 | Wyeth Corp | Metodos para aislar o purificar un producto que comprende poner el producto enlazado en contacto con al menos una solucion de lavado que comprende arginina y luego eluir el producto; y dicho producto. |
| ATE546520T1 (de) * | 2007-01-04 | 2012-03-15 | Crucell Holland Bv | Faktor-xi-reinigung |
| CN104212799B (zh) | 2008-10-15 | 2018-11-23 | Ionis制药公司 | 因子11表达的调节 |
| FR2974301B1 (fr) * | 2011-04-20 | 2013-08-23 | Lab Francais Du Fractionnement | Procede de preparation d'un produit plasmatique deplete en un ou plusieurs facteurs thrombogenes |
| FR2974366B1 (fr) * | 2011-04-20 | 2016-06-24 | Lab Francais Du Fractionnement | Procede de preparation d'un concentre de facteur xi |
| IL212911A0 (en) | 2011-05-16 | 2011-07-31 | Omrix Biopharmaceuticals Ltd | Immunoglobulin reduced in thrombogenic contaminants and preparation thereof |
| DE102012022234A1 (de) | 2012-11-14 | 2014-05-15 | Instraction Gmbh | Einstufiges Verfahren zur Reinigung von (Blut)Plasmaproteinen wie Albumin aus Gemischen |
| DE102012022233A1 (de) | 2012-11-14 | 2014-05-15 | Instraction Gmbh | Verfahren zur Reinigung eines (Blut)plasmaproteins |
| FR3032621A1 (fr) | 2015-02-13 | 2016-08-19 | Lab Francais Du Fractionnement | Colle biologique et son utilisation comme medicament |
| KR101941974B1 (ko) * | 2016-11-18 | 2019-01-24 | 주식회사 녹십자 | 혈장 단백질 정제시 fxi의 제거방법 |
| US20210355497A1 (en) | 2018-05-09 | 2021-11-18 | Ionis Pharmaceuticals, Inc. | Compounds and methods for reducing fxi expression |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4783262A (en) | 1987-03-30 | 1988-11-08 | Cuno Incorporated | Separator for cell type filter element |
| US4859340A (en) | 1976-03-15 | 1989-08-22 | Cuno, Incorporated | Filter sheet |
-
1991
- 1991-05-07 FR FR9105572A patent/FR2676231A1/fr active Granted
- 1991-09-25 IL IL9956791A patent/IL99567A/en not_active IP Right Cessation
-
1992
- 1992-04-23 ES ES92401157T patent/ES2107511T3/es not_active Expired - Lifetime
- 1992-04-23 DK DK92401157.0T patent/DK0512883T3/da active
- 1992-04-23 DE DE69221369T patent/DE69221369T2/de not_active Expired - Lifetime
- 1992-04-23 AT AT92401157T patent/ATE156360T1/de active
- 1992-04-23 EP EP92401157A patent/EP0512883B1/fr not_active Expired - Lifetime
- 1992-04-29 AU AU15263/92A patent/AU652043B2/en not_active Expired
- 1992-05-06 RU SU925011788A patent/RU2097047C1/ru active
- 1992-05-06 CA CA002068069A patent/CA2068069C/en not_active Expired - Lifetime
- 1992-05-07 BR BR929201718A patent/BR9201718A/pt not_active Application Discontinuation
- 1992-05-07 US US07/879,273 patent/US5252217A/en not_active Expired - Lifetime
- 1992-12-29 LT LTIP265A patent/LT3417B/lt not_active IP Right Cessation
-
1993
- 1993-05-21 UA UA93002714A patent/UA27733C2/uk unknown
-
1994
- 1994-05-23 EE EE9400003A patent/EE03017B1/xx not_active IP Right Cessation
-
1997
- 1997-10-22 GR GR970402766T patent/GR3025134T3/el unknown
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4859340A (en) | 1976-03-15 | 1989-08-22 | Cuno, Incorporated | Filter sheet |
| US4783262A (en) | 1987-03-30 | 1988-11-08 | Cuno Incorporated | Separator for cell type filter element |
Non-Patent Citations (4)
| Title |
|---|
| B. HOROWITZ PHD ET AL.: "Inactivation of viruses in labile blood derivatives. I. Disruption of lipid-enveloped viruses by tri(n-butyl)phosphate detergent combinations", TRANSFUSION, 1985, pages 516 - 522, XP002950839, DOI: doi:10.1046/j.1537-2995.1985.25686071422.x |
| BOUMA BN, GRIFFIN JH: "Human blood coagulation factor XI. Purification, properties, and mechanism of activation by activated factor XII", J BIOL CHEM., 1977, pages 6432 - 6437, XP002627223 |
| KOIDE ET AL.: "Blood clotting enzymes", METHODS IN ENZYMOLOGY, 1975, pages 65 - 73 |
| WINKELMAN ET AL.: "Internat" |
Also Published As
| Publication number | Publication date |
|---|---|
| ATE156360T1 (de) | 1997-08-15 |
| EP0512883A1 (fr) | 1992-11-11 |
| EE03017B1 (et) | 1997-08-15 |
| CA2068069A1 (en) | 1992-11-08 |
| RU2097047C1 (ru) | 1997-11-27 |
| BR9201718A (pt) | 1992-12-29 |
| AU652043B2 (en) | 1994-08-11 |
| IL99567A (en) | 1996-01-19 |
| DE69221369D1 (de) | 1997-09-11 |
| DE69221369T2 (de) | 1998-03-19 |
| UA27733C2 (uk) | 2000-10-16 |
| IL99567A0 (en) | 1992-08-18 |
| FR2676231A1 (fr) | 1992-11-13 |
| DK0512883T3 (da) | 1998-03-16 |
| FR2676231B1 (OSRAM) | 1995-04-21 |
| AU1526392A (en) | 1992-11-12 |
| EP0512883B1 (fr) | 1997-08-06 |
| ES2107511T3 (es) | 1997-12-01 |
| US5252217A (en) | 1993-10-12 |
| GR3025134T3 (en) | 1998-02-27 |
| CA2068069C (en) | 2005-03-15 |
| LTIP265A (en) | 1994-10-25 |
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Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| PC9A | Transfer of patents |
Owner name: THE LABORATOIRE FRANCAIS DU FRACTIONNEMENT ET DES Effective date: 20090511 |
|
| TC9A | Change of representative |
Representative=s name: ZABOLIENE, REDA, LT |
|
| MM9A | Lapsed patents |
Effective date: 20091229 |