NL192665C - Weefselkleefstof met een gehalte aan factor XIII en fibrinogeen. - Google Patents
Weefselkleefstof met een gehalte aan factor XIII en fibrinogeen. Download PDFInfo
- Publication number
- NL192665C NL192665C NL8202982A NL8202982A NL192665C NL 192665 C NL192665 C NL 192665C NL 8202982 A NL8202982 A NL 8202982A NL 8202982 A NL8202982 A NL 8202982A NL 192665 C NL192665 C NL 192665C
- Authority
- NL
- Netherlands
- Prior art keywords
- fibrinogen
- factor xiii
- tissue adhesive
- tissue
- present
- Prior art date
Links
- 108010049003 Fibrinogen Proteins 0.000 title claims description 53
- 102000008946 Fibrinogen Human genes 0.000 title claims description 53
- 229940012952 fibrinogen Drugs 0.000 title claims description 52
- 239000003106 tissue adhesive Substances 0.000 title claims description 47
- 108010071289 Factor XIII Proteins 0.000 title claims description 43
- 229940012444 factor xiii Drugs 0.000 title claims description 43
- 230000003115 biocidal effect Effects 0.000 claims description 18
- 108090000190 Thrombin Proteins 0.000 claims description 15
- 229960004072 thrombin Drugs 0.000 claims description 15
- 238000002360 preparation method Methods 0.000 claims description 10
- 239000003242 anti bacterial agent Substances 0.000 claims description 9
- 102000010752 Plasminogen Inactivators Human genes 0.000 claims description 6
- 108010077971 Plasminogen Inactivators Proteins 0.000 claims description 6
- 239000002797 plasminogen activator inhibitor Substances 0.000 claims description 6
- 235000018102 proteins Nutrition 0.000 claims description 6
- 108090000623 proteins and genes Proteins 0.000 claims description 6
- 102000004169 proteins and genes Human genes 0.000 claims description 6
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 claims description 5
- 229940122791 Plasmin inhibitor Drugs 0.000 claims description 5
- 239000011575 calcium Substances 0.000 claims description 5
- 229910052791 calcium Inorganic materials 0.000 claims description 5
- 239000002806 plasmin inhibitor Substances 0.000 claims description 5
- 235000021120 animal protein Nutrition 0.000 claims description 4
- YMDXZJFXQJVXBF-STHAYSLISA-N fosfomycin Chemical compound C[C@@H]1O[C@@H]1P(O)(O)=O YMDXZJFXQJVXBF-STHAYSLISA-N 0.000 claims description 3
- 239000004098 Tetracycline Substances 0.000 claims description 2
- 229940126575 aminoglycoside Drugs 0.000 claims description 2
- 229920001184 polypeptide Polymers 0.000 claims description 2
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 2
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 2
- 229960002180 tetracycline Drugs 0.000 claims description 2
- 229930101283 tetracycline Natural products 0.000 claims description 2
- 235000019364 tetracycline Nutrition 0.000 claims description 2
- 150000003522 tetracyclines Chemical class 0.000 claims description 2
- 150000003952 β-lactams Chemical class 0.000 claims description 2
- 239000000243 solution Substances 0.000 description 19
- 229930182566 Gentamicin Natural products 0.000 description 11
- CEAZRRDELHUEMR-URQXQFDESA-N Gentamicin Chemical compound O1[C@H](C(C)NC)CC[C@@H](N)[C@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](NC)[C@@](C)(O)CO2)O)[C@H](N)C[C@@H]1N CEAZRRDELHUEMR-URQXQFDESA-N 0.000 description 11
- 102000009123 Fibrin Human genes 0.000 description 10
- 108010073385 Fibrin Proteins 0.000 description 10
- BWGVNKXGVNDBDI-UHFFFAOYSA-N Fibrin monomer Chemical compound CNC(=O)CNC(=O)CN BWGVNKXGVNDBDI-UHFFFAOYSA-N 0.000 description 10
- 238000004132 cross linking Methods 0.000 description 10
- 229950003499 fibrin Drugs 0.000 description 10
- 230000001070 adhesive effect Effects 0.000 description 8
- 239000000853 adhesive Substances 0.000 description 7
- 238000000034 method Methods 0.000 description 7
- 239000000203 mixture Substances 0.000 description 7
- 229940075469 tissue adhesives Drugs 0.000 description 7
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 6
- 206010052428 Wound Diseases 0.000 description 6
- 208000027418 Wounds and injury Diseases 0.000 description 6
- 239000001110 calcium chloride Substances 0.000 description 6
- 229910001628 calcium chloride Inorganic materials 0.000 description 6
- 210000001519 tissue Anatomy 0.000 description 6
- 125000000175 2-thienyl group Chemical group S1C([*])=C([H])C([H])=C1[H] 0.000 description 4
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 4
- 230000000845 anti-microbial effect Effects 0.000 description 4
- 239000004599 antimicrobial Substances 0.000 description 4
- 239000007853 buffer solution Substances 0.000 description 4
- 230000000694 effects Effects 0.000 description 4
- 239000000463 material Substances 0.000 description 4
- 210000002381 plasma Anatomy 0.000 description 4
- 239000002244 precipitate Substances 0.000 description 4
- 229940088710 antibiotic agent Drugs 0.000 description 3
- 210000000988 bone and bone Anatomy 0.000 description 3
- YGBFLZPYDUKSPT-MRVPVSSYSA-N cephalosporanic acid Chemical compound S1CC(COC(=O)C)=C(C(O)=O)N2C(=O)C[C@H]21 YGBFLZPYDUKSPT-MRVPVSSYSA-N 0.000 description 3
- 239000004471 Glycine Substances 0.000 description 2
- 241001465754 Metazoa Species 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 2
- 108010000499 Thromboplastin Proteins 0.000 description 2
- 102000002262 Thromboplastin Human genes 0.000 description 2
- 125000000738 acetamido group Chemical group [H]C([H])([H])C(=O)N([H])[*] 0.000 description 2
- 238000006243 chemical reaction Methods 0.000 description 2
- 229960002449 glycine Drugs 0.000 description 2
- 238000007689 inspection Methods 0.000 description 2
- 239000000843 powder Substances 0.000 description 2
- 235000019333 sodium laurylsulphate Nutrition 0.000 description 2
- 238000010257 thawing Methods 0.000 description 2
- 238000005406 washing Methods 0.000 description 2
- 230000029663 wound healing Effects 0.000 description 2
- 206010000369 Accident Diseases 0.000 description 1
- 108010039627 Aprotinin Proteins 0.000 description 1
- GNWUOVJNSFPWDD-XMZRARIVSA-M Cefoxitin sodium Chemical compound [Na+].N([C@]1(OC)C(N2C(=C(COC(N)=O)CS[C@@H]21)C([O-])=O)=O)C(=O)CC1=CC=CS1 GNWUOVJNSFPWDD-XMZRARIVSA-M 0.000 description 1
- KRKNYBCHXYNGOX-UHFFFAOYSA-K Citrate Chemical compound [O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O KRKNYBCHXYNGOX-UHFFFAOYSA-K 0.000 description 1
- 108010080865 Factor XII Proteins 0.000 description 1
- 102000000429 Factor XII Human genes 0.000 description 1
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 1
- 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 description 1
- 229930193140 Neomycin Natural products 0.000 description 1
- 206010031252 Osteomyelitis Diseases 0.000 description 1
- QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 description 1
- 208000031737 Tissue Adhesions Diseases 0.000 description 1
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 239000013543 active substance Substances 0.000 description 1
- 230000002411 adverse Effects 0.000 description 1
- 229960002684 aminocaproic acid Drugs 0.000 description 1
- 229960004405 aprotinin Drugs 0.000 description 1
- JTWOMNBEOCYFNV-NFFDBFGFSA-N azlocillin Chemical compound N([C@@H](C(=O)N[C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C=1C=CC=CC=1)C(=O)N1CCNC1=O JTWOMNBEOCYFNV-NFFDBFGFSA-N 0.000 description 1
- 229960003623 azlocillin Drugs 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 239000004202 carbamide Substances 0.000 description 1
- 229960002682 cefoxitin Drugs 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 230000015271 coagulation Effects 0.000 description 1
- 238000005345 coagulation Methods 0.000 description 1
- 230000000052 comparative effect Effects 0.000 description 1
- 239000012141 concentrate Substances 0.000 description 1
- 230000007423 decrease Effects 0.000 description 1
- 230000007547 defect Effects 0.000 description 1
- 210000003918 fraction a Anatomy 0.000 description 1
- 230000008014 freezing Effects 0.000 description 1
- 238000007710 freezing Methods 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- 229960001031 glucose Drugs 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- 230000023597 hemostasis Effects 0.000 description 1
- 229960002897 heparin Drugs 0.000 description 1
- 229920000669 heparin Polymers 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 230000000937 inactivator Effects 0.000 description 1
- ZPNFWUPYTFPOJU-LPYSRVMUSA-N iniprol Chemical compound C([C@H]1C(=O)NCC(=O)NCC(=O)N[C@H]2CSSC[C@H]3C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C(N[C@H](C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC=4C=CC=CC=4)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC=4C=CC=CC=4)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC2=O)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)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC=2C=CC=CC=2)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H]2N(CCC2)C(=O)[C@@H](N)CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N2[C@@H](CCC2)C(=O)N2[C@@H](CCC2)C(=O)N[C@@H](CC=2C=CC(O)=CC=2)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N2[C@@H](CCC2)C(=O)N3)C(=O)NCC(=O)NCC(=O)N[C@@H](C)C(O)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@H](C(=O)N1)C(C)C)[C@@H](C)O)[C@@H](C)CC)=O)[C@@H](C)CC)C1=CC=C(O)C=C1 ZPNFWUPYTFPOJU-LPYSRVMUSA-N 0.000 description 1
- 230000000977 initiatory effect Effects 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 230000005923 long-lasting effect Effects 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 229960004927 neomycin Drugs 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 230000002085 persistent effect Effects 0.000 description 1
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 230000001737 promoting effect Effects 0.000 description 1
- 238000006894 reductive elimination reaction Methods 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 238000007789 sealing Methods 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 210000003813 thumb Anatomy 0.000 description 1
- 229960000707 tobramycin Drugs 0.000 description 1
- NLVFBUXFDBBNBW-PBSUHMDJSA-N tobramycin Chemical compound N[C@@H]1C[C@H](O)[C@@H](CN)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](N)[C@H](O)[C@@H](CO)O2)O)[C@H](N)C[C@@H]1N NLVFBUXFDBBNBW-PBSUHMDJSA-N 0.000 description 1
- GYDJEQRTZSCIOI-LJGSYFOKSA-N tranexamic acid Chemical compound NC[C@H]1CC[C@H](C(O)=O)CC1 GYDJEQRTZSCIOI-LJGSYFOKSA-N 0.000 description 1
- 229960000401 tranexamic acid Drugs 0.000 description 1
- 239000002753 trypsin inhibitor Substances 0.000 description 1
- 238000010792 warming Methods 0.000 description 1
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 1
Classifications
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61L—METHODS OR APPARATUS FOR STERILISING MATERIALS OR OBJECTS IN GENERAL; DISINFECTION, STERILISATION OR DEODORISATION OF AIR; CHEMICAL ASPECTS OF BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES; MATERIALS FOR BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES
- A61L24/00—Surgical adhesives or cements; Adhesives for colostomy devices
- A61L24/04—Surgical adhesives or cements; Adhesives for colostomy devices containing macromolecular materials
- A61L24/10—Polypeptides; Proteins
- A61L24/106—Fibrin; Fibrinogen
Landscapes
- Health & Medical Sciences (AREA)
- Public Health (AREA)
- Epidemiology (AREA)
- Life Sciences & Earth Sciences (AREA)
- Animal Behavior & Ethology (AREA)
- General Health & Medical Sciences (AREA)
- Surgery (AREA)
- Veterinary Medicine (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Materials For Medical Uses (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
- Peptides Or Proteins (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| AT333781 | 1981-07-28 | ||
| AT0333781A AT369990B (de) | 1981-07-28 | 1981-07-28 | Verfahren zur herstellung eines gewebeklebstoffes |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| NL8202982A NL8202982A (nl) | 1983-02-16 |
| NL192665B NL192665B (nl) | 1997-08-01 |
| NL192665C true NL192665C (nl) | 1997-12-02 |
Family
ID=3548998
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| NL8202982A NL192665C (nl) | 1981-07-28 | 1982-07-23 | Weefselkleefstof met een gehalte aan factor XIII en fibrinogeen. |
Country Status (14)
| Country | Link |
|---|---|
| JP (1) | JPH0696039B2 (cs) |
| AR (1) | AR227252A1 (cs) |
| AT (1) | AT369990B (cs) |
| BE (1) | BE893851A (cs) |
| CA (1) | CA1168982A (cs) |
| CH (1) | CH659187B (cs) |
| DE (1) | DE3225102A1 (cs) |
| DK (1) | DK157977C (cs) |
| ES (1) | ES8306023A1 (cs) |
| FR (1) | FR2510408B1 (cs) |
| GB (1) | GB2102811B (cs) |
| IT (1) | IT1157313B (cs) |
| NL (1) | NL192665C (cs) |
| SE (1) | SE459848B (cs) |
Families Citing this family (32)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH06102628B2 (ja) * | 1984-03-27 | 1994-12-14 | イムノ・アクチエンゲゼルシャフト | 組織接着材の製法 |
| JPS6185304A (ja) * | 1984-10-01 | 1986-04-30 | Green Cross Corp:The | 歯槽骨用材料 |
| DE3622642A1 (de) * | 1986-07-05 | 1988-01-14 | Behringwerke Ag | Einkomponenten-gewebekleber sowie verfahren zu seiner herstellung |
| AT397203B (de) * | 1988-05-31 | 1994-02-25 | Immuno Ag | Gewebeklebstoff |
| US4837379A (en) * | 1988-06-02 | 1989-06-06 | Organogenesis Inc. | Fibrin-collagen tissue equivalents and methods for preparation thereof |
| NZ229385A (en) * | 1989-06-01 | 1992-02-25 | Life Technologies Inc | Treatment of processed fish product (surimi) with alpha-2-macroglobulin to neutralise alkaline proteases in the fish |
| IT1243180B (it) * | 1990-07-31 | 1994-05-24 | Nunzio Rapisarda | Uso della fosfomicina e dei suoi sali come agente cicatrizzante topico |
| US6197325B1 (en) | 1990-11-27 | 2001-03-06 | The American National Red Cross | Supplemented and unsupplemented tissue sealants, methods of their production and use |
| US6117425A (en) * | 1990-11-27 | 2000-09-12 | The American National Red Cross | Supplemented and unsupplemented tissue sealants, method of their production and use |
| US7208179B1 (en) | 1990-11-27 | 2007-04-24 | The American National Red Cross | Methods for treating disease and forming a supplemented fibrin matrix |
| US6559119B1 (en) | 1990-11-27 | 2003-05-06 | Loyola University Of Chicago | Method of preparing a tissue sealant-treated biomedical material |
| US6054122A (en) * | 1990-11-27 | 2000-04-25 | The American National Red Cross | Supplemented and unsupplemented tissue sealants, methods of their production and use |
| AU4566893A (en) * | 1992-07-18 | 1994-02-14 | Opperbas Holding B.V. | A two component fibrin-glue composition for improving in vitro fertilization |
| US5330974A (en) * | 1993-03-01 | 1994-07-19 | Fibratek, Inc. | Therapeutic fibrinogen compositions |
| EP0696201B2 (en) † | 1993-03-12 | 2012-09-19 | The American National Red Cross | Supplemented tissue sealants, methods of their production and use |
| DE69422165T2 (de) * | 1993-03-30 | 2001-10-04 | Omrix Biopharmaceuticals S.A., Bruessel/Bruxelles | Zweikomponenten-fibrinkleber |
| DE19521324C1 (de) * | 1995-06-12 | 1996-10-31 | Immuno Ag | Gewebeklebstoff und Verwendung desselben als Hämostyptikum |
| DE19617369A1 (de) * | 1996-04-30 | 1997-11-06 | Immuno Ag | Lagerstabile Fibrinogen-Präparate |
| AT406120B (de) | 1997-08-28 | 2000-02-25 | Immuno Ag | Gewebekleber |
| AT407484B (de) | 1997-11-12 | 2001-03-26 | Bio Prod & Bio Eng Ag | Arzneimittel zur förderung der wundheilung |
| US6762336B1 (en) | 1998-01-19 | 2004-07-13 | The American National Red Cross | Hemostatic sandwich bandage |
| ES2327208T3 (es) | 1999-12-23 | 2009-10-27 | Csl Limited | Separacion de fibrinogeno de proteasas de plasma. |
| US6506365B1 (en) | 2000-09-25 | 2003-01-14 | Baxter Aktiengesellschaft | Fibrin/fibrinogen binding conjugate |
| IL144446A0 (en) * | 2001-07-19 | 2002-05-23 | Prochon Biotech Ltd | Plasma protein matrices and methods for their preparation |
| CN1327905C (zh) | 2002-09-10 | 2007-07-25 | 美国国家红十字会 | 止血敷料 |
| EP1784415A2 (en) | 2004-08-27 | 2007-05-16 | Novo Nordisk Health Care AG | Purification of factor xiii polypeptides from biological materials |
| ES2378777T3 (es) | 2004-11-23 | 2012-04-17 | Zymogenetics, Inc. | Purificación del factor XIII humano recombinante |
| EP1926459B1 (en) | 2005-09-19 | 2015-01-07 | Histogenics Corporation | Cell-support matrix having narrowly defined uniformly vertically and non-randomly organized porosity and pore density and a method for preparation thereof |
| MX2009001323A (es) | 2006-08-04 | 2009-07-22 | Stb Lifesaving Technologies In | Aposito solido para tratar tejido herido. |
| US20090075891A1 (en) | 2007-08-06 | 2009-03-19 | Macphee Martin | Methods and dressings for sealing internal injuries |
| US10077420B2 (en) | 2014-12-02 | 2018-09-18 | Histogenics Corporation | Cell and tissue culture container |
| US12472237B2 (en) | 2021-12-30 | 2025-11-18 | Baxter International Inc. | Fibrinogen and thrombin solutions for a fibrin sealant and fibrin sealant kit |
Family Cites Families (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| AT359653B (de) * | 1979-02-15 | 1980-11-25 | Immuno Ag | Verfahren zur herstellung eines gewebekleb- stoffes |
| AT359652B (de) * | 1979-02-15 | 1980-11-25 | Immuno Ag | Verfahren zur herstellung eines gewebekleb- stoffes |
| WO1981000516A1 (fr) * | 1979-08-31 | 1981-03-05 | Merck Patent Gmbh | Gel contenant fibrine et antibiotique pour le traitement d'os infectes et son procede de preparation |
-
1981
- 1981-07-28 AT AT0333781A patent/AT369990B/de not_active IP Right Cessation
-
1982
- 1982-07-01 SE SE8204064A patent/SE459848B/sv not_active IP Right Cessation
- 1982-07-05 DK DK300682A patent/DK157977C/da active
- 1982-07-05 CH CH409482A patent/CH659187B/de unknown
- 1982-07-05 DE DE19823225102 patent/DE3225102A1/de active Granted
- 1982-07-06 GB GB08219500A patent/GB2102811B/en not_active Expired
- 1982-07-13 CA CA000407154A patent/CA1168982A/en not_active Expired
- 1982-07-16 BE BE0/208601A patent/BE893851A/fr not_active IP Right Cessation
- 1982-07-21 AR AR290039A patent/AR227252A1/es active
- 1982-07-22 JP JP57126829A patent/JPH0696039B2/ja not_active Expired - Lifetime
- 1982-07-23 NL NL8202982A patent/NL192665C/nl not_active IP Right Cessation
- 1982-07-23 FR FR8212918A patent/FR2510408B1/fr not_active Expired
- 1982-07-27 ES ES514441A patent/ES8306023A1/es not_active Expired
- 1982-07-27 IT IT22595/82A patent/IT1157313B/it active
Also Published As
| Publication number | Publication date |
|---|---|
| AR227252A1 (es) | 1982-09-30 |
| DE3225102A1 (de) | 1983-02-17 |
| ES514441A0 (es) | 1983-05-01 |
| SE459848B (sv) | 1989-08-14 |
| IT1157313B (it) | 1987-02-11 |
| NL192665B (nl) | 1997-08-01 |
| CA1168982A (en) | 1984-06-12 |
| DK157977C (da) | 1990-08-13 |
| JPH0696039B2 (ja) | 1994-11-30 |
| DE3225102C2 (cs) | 1990-05-31 |
| AT369990B (de) | 1983-02-25 |
| FR2510408B1 (fr) | 1987-02-27 |
| SE8204064L (sv) | 1983-01-29 |
| ATA333781A (de) | 1982-07-15 |
| IT8222595A0 (it) | 1982-07-27 |
| GB2102811A (en) | 1983-02-09 |
| BE893851A (fr) | 1982-11-16 |
| NL8202982A (nl) | 1983-02-16 |
| CH659187B (cs) | 1987-01-15 |
| JPS5826821A (ja) | 1983-02-17 |
| DK157977B (da) | 1990-03-12 |
| FR2510408A1 (fr) | 1983-02-04 |
| ES8306023A1 (es) | 1983-05-01 |
| DK300682A (da) | 1983-01-29 |
| SE8204064D0 (sv) | 1982-07-01 |
| GB2102811B (en) | 1985-01-30 |
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