FI104378B - Menetelmä trombiinin valmistamiseksi - Google Patents

Menetelmä trombiinin valmistamiseksi Download PDF

Info

Publication number: FI104378B
Authority: FI; Finland
Prior art keywords: thrombin; prothrombin; complex; virus; factor
Prior art date: 1991-11-04

Application number

FI924975A

Other languages

English (en)

Finnish (fi)

Swedish (sv)

Other versions

FI924975A0 (fi

FI924975L (fi

Inventor

Johann Eibl

Yendra Linnau

Original Assignee

Baxter Ag

Priority date (The priority date 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 date listed.)

1991-11-04

Filing date

1992-11-04

Publication date

2000-01-14

Family has litigation

First worldwide family litigation filed litigation Critical https://patents.darts-ip.com/?family=3529491&utm_source=google_patent&utm_medium=platform_link&utm_campaign=public_patent_search&patent=FI104378(B) "Global patent litigation dataset” by Darts-ip is licensed under a Creative Commons Attribution 4.0 International License.

1992-11-04 Application filed by Baxter Ag filed Critical Baxter Ag

1992-11-04 Publication of FI924975A0 publication Critical patent/FI924975A0/fi

1993-05-05 Publication of FI924975L publication Critical patent/FI924975L/fi

2000-01-14 Application granted granted Critical

2000-01-14 Publication of FI104378B publication Critical patent/FI104378B/fi

Links

108090000190 Thrombin Proteins 0.000 title claims abstract description 40
229960004072 thrombin Drugs 0.000 title claims abstract description 38
238000000034 method Methods 0.000 title claims description 9
108010094028 Prothrombin Proteins 0.000 claims abstract description 32
102100027378 Prothrombin Human genes 0.000 claims abstract description 27
229940039716 prothrombin Drugs 0.000 claims abstract description 27
239000012678 infectious agent Substances 0.000 claims abstract description 8
238000004519 manufacturing process Methods 0.000 claims description 3
238000001042 affinity chromatography Methods 0.000 claims description 2
238000004255 ion exchange chromatography Methods 0.000 claims description 2
230000003213 activating effect Effects 0.000 claims 2
230000000415 inactivating effect Effects 0.000 claims 1
230000004913 activation Effects 0.000 abstract description 10
241001465754 Metazoa Species 0.000 abstract description 4
238000010438 heat treatment Methods 0.000 abstract description 3
230000000694 effects Effects 0.000 description 9
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 7
210000002381 plasma Anatomy 0.000 description 7
150000003839 salts Chemical class 0.000 description 6
BHPQYMZQTOCNFJ-UHFFFAOYSA-N Calcium cation Chemical compound [Ca+2] BHPQYMZQTOCNFJ-UHFFFAOYSA-N 0.000 description 5
108010074860 Factor Xa Proteins 0.000 description 5
239000011575 calcium Substances 0.000 description 5
229910001424 calcium ion Inorganic materials 0.000 description 5
AGVAZMGAQJOSFJ-WZHZPDAFSA-M cobalt(2+);[(2r,3s,4r,5s)-5-(5,6-dimethylbenzimidazol-1-yl)-4-hydroxy-2-(hydroxymethyl)oxolan-3-yl] [(2r)-1-[3-[(1r,2r,3r,4z,7s,9z,12s,13s,14z,17s,18s,19r)-2,13,18-tris(2-amino-2-oxoethyl)-7,12,17-tris(3-amino-3-oxopropyl)-3,5,8,8,13,15,18,19-octamethyl-2 Chemical compound [Co+2].N#[C-].[N-]([C@@H]1[C@H](CC(N)=O)[C@@]2(C)CCC(=O)NC[C@@H](C)OP(O)(=O)O[C@H]3[C@H]([C@H](O[C@@H]3CO)N3C4=CC(C)=C(C)C=C4N=C3)O)\C2=C(C)/C([C@H](C\2(C)C)CCC(N)=O)=N/C/2=C\C([C@H]([C@@]/2(CC(N)=O)C)CCC(N)=O)=N\C\2=C(C)/C2=N[C@]1(C)[C@@](C)(CC(N)=O)[C@@H]2CCC(N)=O AGVAZMGAQJOSFJ-WZHZPDAFSA-M 0.000 description 5
108010039209 Blood Coagulation Factors Proteins 0.000 description 4
102000015081 Blood Coagulation Factors Human genes 0.000 description 4
OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 4
206010053567 Coagulopathies Diseases 0.000 description 4
239000003114 blood coagulation factor Substances 0.000 description 4
229910052791 calcium Inorganic materials 0.000 description 4
230000035602 clotting Effects 0.000 description 4
241000700605 Viruses Species 0.000 description 3
238000006243 chemical reaction Methods 0.000 description 3
238000011109 contamination Methods 0.000 description 3
238000002360 preparation method Methods 0.000 description 3
239000011780 sodium chloride Substances 0.000 description 3
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 2
108010014172 Factor V Proteins 0.000 description 2
102000009123 Fibrin Human genes 0.000 description 2
108010073385 Fibrin Proteins 0.000 description 2
BWGVNKXGVNDBDI-UHFFFAOYSA-N Fibrin monomer Chemical compound CNC(=O)CNC(=O)CN BWGVNKXGVNDBDI-UHFFFAOYSA-N 0.000 description 2
108010049003 Fibrinogen Proteins 0.000 description 2
102000008946 Fibrinogen Human genes 0.000 description 2
KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 2
239000004472 Lysine Substances 0.000 description 2
229920002684 Sepharose Polymers 0.000 description 2
230000002411 adverse Effects 0.000 description 2
108010018823 anti-inhibitor coagulant complex Proteins 0.000 description 2
238000001816 cooling Methods 0.000 description 2
238000011026 diafiltration Methods 0.000 description 2
238000002474 experimental method Methods 0.000 description 2
229940105776 factor viii inhibitor bypassing activity Drugs 0.000 description 2
229950003499 fibrin Drugs 0.000 description 2
229940012952 fibrinogen Drugs 0.000 description 2
239000011159 matrix material Substances 0.000 description 2
239000000825 pharmaceutical preparation Substances 0.000 description 2
150000003904 phospholipids Chemical class 0.000 description 2
102000004169 proteins and genes Human genes 0.000 description 2
108090000623 proteins and genes Proteins 0.000 description 2
108010014806 prothrombinase complex Proteins 0.000 description 2
239000003381 stabilizer Substances 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
241000283690 Bos taurus Species 0.000 description 1
108010062466 Enzyme Precursors Proteins 0.000 description 1
102000010911 Enzyme Precursors Human genes 0.000 description 1
101001038021 Lonomia obliqua Lopap Proteins 0.000 description 1
102000006833 Multifunctional Enzymes Human genes 0.000 description 1
108010047290 Multifunctional Enzymes Proteins 0.000 description 1
108091005804 Peptidases Proteins 0.000 description 1
102000035195 Peptidases Human genes 0.000 description 1
239000004365 Protease Substances 0.000 description 1
229920005654 Sephadex Polymers 0.000 description 1
239000012507 Sephadex™ Substances 0.000 description 1
VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 1
108010000499 Thromboplastin Proteins 0.000 description 1
102000002262 Thromboplastin Human genes 0.000 description 1
PTFCDOFLOPIGGS-UHFFFAOYSA-N Zinc dication Chemical compound [Zn+2] PTFCDOFLOPIGGS-UHFFFAOYSA-N 0.000 description 1
239000012190 activator Substances 0.000 description 1
150000001450 anions Chemical class 0.000 description 1
230000004071 biological effect Effects 0.000 description 1
230000015572 biosynthetic process Effects 0.000 description 1
230000000740 bleeding effect Effects 0.000 description 1
230000023555 blood coagulation Effects 0.000 description 1
229940019700 blood coagulation factors Drugs 0.000 description 1
239000003795 chemical substances by application Substances 0.000 description 1
239000003593 chromogenic compound Substances 0.000 description 1
238000003776 cleavage reaction Methods 0.000 description 1
230000001112 coagulating effect Effects 0.000 description 1
230000000959 cryoprotective effect Effects 0.000 description 1
108010074164 cyclohexylglycyl-alanyl-arginine-4-nitroanilide Proteins 0.000 description 1
239000000032 diagnostic agent Substances 0.000 description 1
229940039227 diagnostic agent Drugs 0.000 description 1
239000003814 drug Substances 0.000 description 1
238000011066 ex-situ storage Methods 0.000 description 1
238000004108 freeze drying Methods 0.000 description 1
239000003292 glue Substances 0.000 description 1
208000006454 hepatitis Diseases 0.000 description 1
231100000283 hepatitis Toxicity 0.000 description 1
230000002779 inactivation Effects 0.000 description 1
150000002500 ions Chemical class 0.000 description 1
239000000463 material Substances 0.000 description 1
239000012528 membrane Substances 0.000 description 1
244000052769 pathogen Species 0.000 description 1
239000011148 porous material Substances 0.000 description 1
238000000746 purification Methods 0.000 description 1
238000011084 recovery Methods 0.000 description 1
230000007017 scission Effects 0.000 description 1
239000001632 sodium acetate Substances 0.000 description 1
235000017281 sodium acetate Nutrition 0.000 description 1
239000001509 sodium citrate Substances 0.000 description 1
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 description 1
239000007858 starting material Substances 0.000 description 1
229910052712 strontium Inorganic materials 0.000 description 1
CIOAGBVUUVVLOB-UHFFFAOYSA-N strontium atom Chemical compound [Sr] CIOAGBVUUVVLOB-UHFFFAOYSA-N 0.000 description 1
238000001356 surgical procedure Methods 0.000 description 1
239000000725 suspension Substances 0.000 description 1
238000002560 therapeutic procedure Methods 0.000 description 1
210000001519 tissue Anatomy 0.000 description 1
230000003612 virological effect Effects 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)
- C12N9/6429—Thrombin (3.4.21.5)
- 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
- 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)
- C12Y304/21005—Thrombin (3.4.21.5)
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides

Landscapes

Health & Medical Sciences (AREA)
Chemical & Material Sciences (AREA)
Engineering & Computer Science (AREA)
Life Sciences & Earth Sciences (AREA)
Organic Chemistry (AREA)
Bioinformatics & Cheminformatics (AREA)
Genetics & Genomics (AREA)
Wood Science & Technology (AREA)
Zoology (AREA)
General Health & Medical Sciences (AREA)
Biochemistry (AREA)
Biomedical Technology (AREA)
General Engineering & Computer Science (AREA)
Medicinal Chemistry (AREA)
Molecular Biology (AREA)
Microbiology (AREA)
Biotechnology (AREA)
Hematology (AREA)
Pharmacology & Pharmacy (AREA)
Veterinary Medicine (AREA)
Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
Public Health (AREA)
General Chemical & Material Sciences (AREA)
Chemical Kinetics & Catalysis (AREA)
Animal Behavior & Ethology (AREA)
Diabetes (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Enzymes And Modification Thereof (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)
Peptides Or Proteins (AREA)
Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
Amplifiers (AREA)
Revetment (AREA)
Ultra Sonic Daignosis Equipment (AREA)
Saccharide Compounds (AREA)

FI924975A 1991-11-04 1992-11-04 Menetelmä trombiinin valmistamiseksi FI104378B (fi)

Applications Claiming Priority (2)

Application Number	Priority Date	Filing Date	Title
AT0218391A AT398079B (de)	1991-11-04	1991-11-04	Präparation mit thrombinaktivität sowie verfahren zu ihrer herstellung
AT218391		1991-11-04

Publications (3)

Publication Number	Publication Date
FI924975A0 FI924975A0 (fi)	1992-11-04
FI924975L FI924975L (fi)	1993-05-05
FI104378B true FI104378B (fi)	2000-01-14

Family

ID=3529491

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
FI924975A FI104378B (fi)	1991-11-04	1992-11-04	Menetelmä trombiinin valmistamiseksi

Country Status (19)

Country	Link
US (1)	US5714370A (fr)
EP (1)	EP0541507B1 (fr)
JP (1)	JP2572513B2 (fr)
AT (2)	AT398079B (fr)
AU (1)	AU645715B2 (fr)
CA (1)	CA2081703C (fr)
CZ (1)	CZ281502B6 (fr)
DE (1)	DE59209922D1 (fr)
DK (1)	DK0541507T3 (fr)
ES (1)	ES2165355T3 (fr)
FI (1)	FI104378B (fr)
HR (1)	HRP921171B1 (fr)
HU (1)	HU213867B (fr)
MX (1)	MX9206303A (fr)
NO (1)	NO312125B1 (fr)
PL (1)	PL170156B1 (fr)
SI (1)	SI9200299B (fr)
SK (1)	SK330992A3 (fr)
YU (1)	YU96192A (fr)

Families Citing this family (48)

* Cited by examiner, † Cited by third party
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AT402891B (de) *	1991-06-20	1997-09-25	Immuno Ag	Verfahren zur herstellung eines inaktivierten blutproduktes
DE4137996A1 (de) *	1991-11-19	1993-05-27	Behringwerke Ag	Verfahren zur herstellung eines virussicheren thrombinkonzentrates
AT399818B (de) *	1992-04-24	1995-07-25	Immuno Ag	Verfahren zur herstellung einer hochgereinigten virussicheren faktor viii-präparation
EP0674531A1 (fr) *	1992-12-16	1995-10-04	IMMUNO Aktiengesellschaft	Procede de preparation de compositions biologiques exemptes de virus
DE4320294A1 (de) *	1993-06-18	1994-12-22	Immuno Ag	Verwendung von humanem Protein C zur Verhinderung und Behandlung von Thrombozytenablagerungen
JPH07308190A (ja) *	1994-05-18	1995-11-28	Green Cross Corp:The	トロンビンの製造方法
US5506127A (en) *	1994-09-21	1996-04-09	Proba; Zbigniew	Therapeutic grade thrombin produced by chromatography
GB9503750D0 (en) *	1995-02-24	1995-04-12	Common Services Agency	Thrombin preparation
AT404597B (de)	1995-11-24	1998-12-28	Immuno Ag	Verfahren zur herstellung von proteinen
JP3944267B2 (ja) *	1996-08-09	2007-07-11	財団法人化学及血清療法研究所	プロトロンビンの活性化方法および該方法に基づくトロンビンの製造方法
US6066325A (en) *	1996-08-27	2000-05-23	Fusion Medical Technologies, Inc.	Fragmented polymeric compositions and methods for their use
US8303981B2 (en)	1996-08-27	2012-11-06	Baxter International Inc.	Fragmented polymeric compositions and methods for their use
US8603511B2 (en)	1996-08-27	2013-12-10	Baxter International, Inc.	Fragmented polymeric compositions and methods for their use
US7435425B2 (en)	2001-07-17	2008-10-14	Baxter International, Inc.	Dry hemostatic compositions and methods for their preparation
AT405608B (de) *	1997-04-08	1999-10-25	Immuno Ag	Verfahren zur inaktivierung von pathogenen, insbesondere von viren, in einem biologischen material
AT405485B (de)	1997-05-28	1999-08-25	Immuno Ag	Eine das vwf-propeptid enthaltende pharmazeutische präparation
AU5903000A (en) *	1999-06-29	2001-01-31	Government Of The United States Of America, As Represented By The Secretary Of The Department Of Health And Human Services, The	Novel anti-thrombin peptide
US7795218B2 (en)	2001-04-12	2010-09-14	Bioaxone Therapeutique Inc.	ADP-ribosyl transferase fusion variant proteins
GB0216002D0 (en) *	2002-07-10	2002-08-21	Nat Blood Authority	Process and composition
US8834864B2 (en) *	2003-06-05	2014-09-16	Baxter International Inc.	Methods for repairing and regenerating human dura mater
US7927626B2 (en)	2003-08-07	2011-04-19	Ethicon, Inc.	Process of making flowable hemostatic compositions and devices containing such compositions
KR20090017654A (ko) *	2006-05-31	2009-02-18	백스터 인터내셔널 인코포레이티드	척수 수술에서 세포 내성장을 통제하고 조직 재생을 조절하는 방법
TWI436793B (zh)	2006-08-02	2014-05-11	巴克斯特國際公司	快速作用之乾密封膠及其使用和製造方法
US8790698B2 (en)	2007-10-30	2014-07-29	Baxter International Inc.	Use of a regenerative biofunctional collagen biomatrix for treating visceral or parietal defects
CN102014973A (zh)	2008-02-29	2011-04-13	弗罗桑医疗设备公司	用于促进止血和/或伤口愈合的装置
TWI488662B (zh)	2008-12-11	2015-06-21	Baxter Int	基於血纖維蛋白元與硫酸化多醣的製劑
KR101105026B1 (ko) *	2009-04-06	2012-01-16	김기영	다방향 굴절형 핸드 그라인더
US9039783B2 (en) *	2009-05-18	2015-05-26	Baxter International, Inc.	Method for the improvement of mesh implant biocompatibility
US9162006B2 (en) *	2009-06-16	2015-10-20	Baxter International Inc.	Hemostatic sponge
WO2011079336A1 (fr) *	2009-12-16	2011-07-07	Baxter International Inc.	Eponge hémostatique
SA111320355B1 (ar)	2010-04-07	2015-01-08	Baxter Heathcare S A	إسفنجة لايقاف النزف
ES2682302T3 (es)	2010-06-01	2018-09-19	Baxter International Inc	Proceso para la producción de composiciones hemostáticas secas y estables
AU2011260260B2 (en)	2010-06-01	2015-09-03	Baxter Healthcare S.A.	Process for making dry and stable hemostatic compositions
MX344402B (es)	2010-06-01	2016-12-14	Baxter Int Inc *	Proceso para elaborar composiciones hemostaticas secas y estables.
HK1201212A1 (en)	2011-10-11	2015-08-28	Baxter International Inc	Hemostatic compositions
ES2938568T3 (es)	2011-10-11	2023-04-12	Baxter Int	Composiciones hemostaticas
SG11201401878SA (en)	2011-10-27	2014-09-26	Baxter Int	Hemostatic compositions
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1991
- 1991-11-04 AT AT0218391A patent/AT398079B/de not_active IP Right Cessation
1992
- 1992-10-27 AU AU27361/92A patent/AU645715B2/en not_active Ceased
- 1992-10-27 HU HU9203366A patent/HU213867B/hu not_active IP Right Cessation
- 1992-10-29 CA CA002081703A patent/CA2081703C/fr not_active Expired - Lifetime
- 1992-11-02 EP EP92890232A patent/EP0541507B1/fr not_active Revoked
- 1992-11-02 HR HRA2183/91A patent/HRP921171B1/xx not_active IP Right Cessation
- 1992-11-02 DE DE59209922T patent/DE59209922D1/de not_active Revoked
- 1992-11-02 DK DK92890232T patent/DK0541507T3/da active
- 1992-11-02 ES ES92890232T patent/ES2165355T3/es not_active Expired - Lifetime
- 1992-11-02 AT AT92890232T patent/ATE206757T1/de not_active IP Right Cessation
- 1992-11-03 PL PL92296460A patent/PL170156B1/pl not_active IP Right Cessation
- 1992-11-03 MX MX9206303A patent/MX9206303A/es unknown
- 1992-11-03 NO NO19924229A patent/NO312125B1/no not_active IP Right Cessation
- 1992-11-04 FI FI924975A patent/FI104378B/fi not_active IP Right Cessation
- 1992-11-04 SI SI9200299A patent/SI9200299B/sl not_active IP Right Cessation
- 1992-11-04 CZ CS923309A patent/CZ281502B6/cs not_active IP Right Cessation
- 1992-11-04 JP JP4294962A patent/JP2572513B2/ja not_active Expired - Fee Related
- 1992-11-04 YU YU96192A patent/YU96192A/sh unknown
- 1992-11-04 SK SK3309-92A patent/SK330992A3/sk unknown
1995
- 1995-06-01 US US08/458,082 patent/US5714370A/en not_active Expired - Lifetime

Also Published As

Publication number	Publication date
PL296460A1 (en)	1993-12-13
SI9200299B (sl)	2002-02-28
AU645715B2 (en)	1994-01-20
CA2081703A1 (fr)	1993-05-05
EP0541507A2 (fr)	1993-05-12
HUT65390A (en)	1994-06-28
CZ281502B6 (cs)	1996-10-16
ES2165355T3 (es)	2002-03-16
DK0541507T3 (da)	2002-01-28
SK279193B6 (sk)	1998-07-08
EP0541507A3 (en)	1993-06-16
SI9200299A (en)	1994-06-30
CA2081703C (fr)	1999-01-19
NO924229L (no)	1993-05-05
JPH0646852A (ja)	1994-02-22
FI924975A0 (fi)	1992-11-04
MX9206303A (es)	1993-08-01
CZ330992A3 (en)	1993-06-16
NO312125B1 (no)	2002-03-25
SK330992A3 (en)	1998-07-08
YU96192A (sh)	1995-12-04
ATE206757T1 (de)	2001-10-15
PL170156B1 (pl)	1996-10-31
AU2736192A (en)	1993-05-06
HRP921171A2 (en)	1995-08-31
FI924975L (fi)	1993-05-05
JP2572513B2 (ja)	1997-01-16
HU213867B (en)	1997-11-28
HU9203366D0 (en)	1993-01-28
DE59209922D1 (de)	2001-11-15
AT398079B (de)	1994-09-26
HRP921171B1 (en)	2000-02-29
EP0541507B1 (fr)	2001-10-10
US5714370A (en)	1998-02-03
ATA218391A (de)	1994-01-15
NO924229D0 (no)	1992-11-03

Legal Events

Date	Code	Title	Description
2006-05-31	MA	Patent expired

Publication	Publication Date	Title
CA2081703C (fr)	1999-01-19	Thrombine et methode permettant de la produire
US4876241A (en)	1989-10-24	Stabilization of biological and pharmaceutical products during thermal inactivation of viral and bacterial contaminants
AU758152B2 (en)	2003-03-13	Pharmaceutical factor VII preparation
US5639730A (en)	1997-06-17	Method of producing a virus-safe biological preparation
AU737566B2 (en)	2001-08-23	An immunotolerant prothrombin complex preparation
AU711298B2 (en)	1999-10-07	Therapeutic grade thrombin production and products
JP4445386B2 (ja)	2010-04-07	ウィルス不活性化トロンビン調製物の製造方法
EP0292003B1 (fr)	1994-03-23	Stabilisation de produits biologiques ou pharmaceutiques pendant l'inactivation des contaminants viraux ou bactériens
SK281266B6 (sk)	2001-01-18	Spôsob získavania enzýmov z proenzýmov
EP0763596A1 (fr)	1997-03-19	Procede pour la production de thrombine
AU739845B2 (en)	2001-10-18	A method for inactivating pathogens, in particular viruses, in a biological material
JP2965069B2 (ja)	1999-10-18	蛋白質含有組成物の製造方法
JP3947247B2 (ja)	2007-07-18	活性蛋白質組成物の製造方法
MXPA99008941A (es)	2000-06-01	Preparacion del complejo de protrombina inmunotolerante