CH681693A5 - - Google Patents
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- Publication number
- CH681693A5 CH681693A5 CH606/91A CH60691A CH681693A5 CH 681693 A5 CH681693 A5 CH 681693A5 CH 606/91 A CH606/91 A CH 606/91A CH 60691 A CH60691 A CH 60691A CH 681693 A5 CH681693 A5 CH 681693A5
- Authority
- CH
- Switzerland
- Prior art keywords
- adhesive
- fibrinogen
- adhesive according
- enzyme
- batroxobin
- Prior art date
Links
- 230000001070 adhesive effect Effects 0.000 claims abstract description 79
- 239000000853 adhesive Substances 0.000 claims abstract description 78
- 108090000790 Enzymes Proteins 0.000 claims abstract description 28
- 102000004190 Enzymes Human genes 0.000 claims abstract description 28
- 108010049003 Fibrinogen Proteins 0.000 claims abstract description 28
- 102000008946 Fibrinogen Human genes 0.000 claims abstract description 28
- 229940012952 fibrinogen Drugs 0.000 claims abstract description 28
- 239000003998 snake venom Substances 0.000 claims abstract description 18
- 239000000126 substance Substances 0.000 claims abstract description 11
- BHPQYMZQTOCNFJ-UHFFFAOYSA-N Calcium cation Chemical compound [Ca+2] BHPQYMZQTOCNFJ-UHFFFAOYSA-N 0.000 claims abstract description 6
- 229910001424 calcium ion Inorganic materials 0.000 claims abstract description 6
- 108010027612 Batroxobin Proteins 0.000 claims description 28
- 229940088598 enzyme Drugs 0.000 claims description 27
- 229960002210 batroxobin Drugs 0.000 claims description 25
- 108010067306 Fibronectins Proteins 0.000 claims description 13
- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 claims description 13
- 108010071289 Factor XIII Proteins 0.000 claims description 11
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 claims description 9
- 108010039627 Aprotinin Proteins 0.000 claims description 8
- 229960004405 aprotinin Drugs 0.000 claims description 8
- 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 claims description 8
- 241000271897 Viperidae Species 0.000 claims description 6
- 239000001110 calcium chloride Substances 0.000 claims description 5
- 229910001628 calcium chloride Inorganic materials 0.000 claims description 5
- 101000623895 Bos taurus Mucin-15 Proteins 0.000 claims description 4
- 229940105784 coagulation factor xiii Drugs 0.000 claims description 4
- 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 claims description 4
- 239000002904 solvent Substances 0.000 claims description 4
- 239000002435 venom Substances 0.000 claims description 4
- 231100000611 venom Toxicity 0.000 claims description 4
- 210000001048 venom Anatomy 0.000 claims description 4
- 108010001779 Ancrod Proteins 0.000 claims description 3
- 241000392415 Bothrops moojeni Species 0.000 claims description 3
- 241000270295 Serpentes Species 0.000 claims description 3
- 239000007864 aqueous solution Substances 0.000 claims description 3
- 239000003638 chemical reducing agent Substances 0.000 claims description 3
- -1 thiol compound Chemical class 0.000 claims description 3
- IMVJCTWESJIARS-ZXZARUISSA-N (2s,3r)-2,3-bis(sulfanyl)butane-1,4-diol Chemical compound OC[C@H](S)[C@H](S)CO IMVJCTWESJIARS-ZXZARUISSA-N 0.000 claims description 2
- 108010024636 Glutathione Proteins 0.000 claims description 2
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 claims description 2
- 102000002933 Thioredoxin Human genes 0.000 claims description 2
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 claims description 2
- 235000018417 cysteine Nutrition 0.000 claims description 2
- 239000008151 electrolyte solution Substances 0.000 claims description 2
- 229960003180 glutathione Drugs 0.000 claims description 2
- 108060008226 thioredoxin Proteins 0.000 claims description 2
- 229940094937 thioredoxin Drugs 0.000 claims description 2
- 102000016359 Fibronectins Human genes 0.000 claims 2
- AOCTYHGSZBKDPD-UHFFFAOYSA-N C1=CC(C)=CC=C1S(=O)(=O)NC(C(=O)NC=1C=CC=CC=1)CCC1=CC=C(C(N)=N)C=C1 Chemical compound C1=CC(C)=CC=C1S(=O)(=O)NC(C(=O)NC=1C=CC=CC=1)CCC1=CC=C(C(N)=N)C=C1 AOCTYHGSZBKDPD-UHFFFAOYSA-N 0.000 claims 1
- 241000271064 Calloselasma rhodostoma Species 0.000 claims 1
- 229940122791 Plasmin inhibitor Drugs 0.000 claims 1
- 239000004227 calcium gluconate Substances 0.000 claims 1
- 229960004494 calcium gluconate Drugs 0.000 claims 1
- 235000013927 calcium gluconate Nutrition 0.000 claims 1
- NEEHYRZPVYRGPP-UHFFFAOYSA-L calcium;2,3,4,5,6-pentahydroxyhexanoate Chemical compound [Ca+2].OCC(O)C(O)C(O)C(O)C([O-])=O.OCC(O)C(O)C(O)C(O)C([O-])=O NEEHYRZPVYRGPP-UHFFFAOYSA-L 0.000 claims 1
- 239000002806 plasmin inhibitor Substances 0.000 claims 1
- 108010000196 Factor XIIIa Proteins 0.000 abstract description 6
- 239000003114 blood coagulation factor Substances 0.000 abstract description 3
- 108090000190 Thrombin Proteins 0.000 description 31
- 229960004072 thrombin Drugs 0.000 description 31
- 239000000243 solution Substances 0.000 description 21
- 210000001519 tissue Anatomy 0.000 description 19
- 239000000203 mixture Substances 0.000 description 15
- 102100037362 Fibronectin Human genes 0.000 description 11
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 10
- 239000003708 ampul Substances 0.000 description 7
- 239000000835 fiber Substances 0.000 description 7
- 229910052751 metal Inorganic materials 0.000 description 7
- 239000002184 metal Substances 0.000 description 7
- 108010073385 Fibrin Proteins 0.000 description 6
- 102000009123 Fibrin Human genes 0.000 description 6
- 238000000034 method Methods 0.000 description 6
- 238000006116 polymerization reaction Methods 0.000 description 6
- BWGVNKXGVNDBDI-UHFFFAOYSA-N Fibrin monomer Chemical compound CNC(=O)CNC(=O)CN BWGVNKXGVNDBDI-UHFFFAOYSA-N 0.000 description 5
- 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 5
- 241000700605 Viruses Species 0.000 description 5
- 206010052428 Wound Diseases 0.000 description 5
- 208000027418 Wounds and injury Diseases 0.000 description 5
- 230000004913 activation Effects 0.000 description 5
- 238000006243 chemical reaction Methods 0.000 description 5
- 230000003511 endothelial effect Effects 0.000 description 5
- 238000002474 experimental method Methods 0.000 description 5
- 229940012444 factor xiii Drugs 0.000 description 5
- 229950003499 fibrin Drugs 0.000 description 5
- 239000000499 gel Substances 0.000 description 5
- 229960002897 heparin Drugs 0.000 description 5
- 229920000669 heparin Polymers 0.000 description 5
- 239000011780 sodium chloride Substances 0.000 description 5
- 239000008280 blood Substances 0.000 description 4
- 210000004369 blood Anatomy 0.000 description 4
- 230000000694 effects Effects 0.000 description 4
- 238000005259 measurement Methods 0.000 description 4
- 235000018102 proteins Nutrition 0.000 description 4
- 102000004169 proteins and genes Human genes 0.000 description 4
- 108090000623 proteins and genes Proteins 0.000 description 4
- 230000009424 thromboembolic effect Effects 0.000 description 4
- 102000004411 Antithrombin III Human genes 0.000 description 3
- 108090000935 Antithrombin III Proteins 0.000 description 3
- 241000283690 Bos taurus Species 0.000 description 3
- 108010080379 Fibrin Tissue Adhesive Proteins 0.000 description 3
- 101800000974 Fibrinopeptide A Proteins 0.000 description 3
- 229960005348 antithrombin iii Drugs 0.000 description 3
- 230000015572 biosynthetic process Effects 0.000 description 3
- 210000004027 cell Anatomy 0.000 description 3
- 229940106780 human fibrinogen Drugs 0.000 description 3
- 229920003002 synthetic resin Polymers 0.000 description 3
- 239000000057 synthetic resin Substances 0.000 description 3
- 238000012360 testing method Methods 0.000 description 3
- 230000001960 triggered effect Effects 0.000 description 3
- JWICNZAGYSIBAR-LEEGLKINSA-N (4s)-4-[[2-[[(2s)-2-[[(2s)-2-[[(2s)-2-aminopropanoyl]amino]-3-carboxypropanoyl]amino]-3-hydroxypropanoyl]amino]acetyl]amino]-5-[[2-[[(2s)-3-carboxy-1-[[(2s)-1-[[1-[[(2s)-1-[[(2s)-4-carboxy-1-[[2-[[2-[[2-[[(2s)-1-[[(1s)-1-carboxy-4-(diaminomethylideneamino Chemical compound NC(N)=NCCC[C@@H](C(O)=O)NC(=O)[C@H](C(C)C)NC(=O)CNC(=O)CNC(=O)CNC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C)NC(=O)C(CC(C)C)NC(=O)[C@@H](NC(=O)[C@H](CC(O)=O)NC(=O)CNC(=O)[C@H](CCC(O)=O)NC(=O)CNC(=O)[C@H](CO)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](C)N)CC1=CC=CC=C1 JWICNZAGYSIBAR-LEEGLKINSA-N 0.000 description 2
- 102000015081 Blood Coagulation Factors Human genes 0.000 description 2
- 108010039209 Blood Coagulation Factors Proteins 0.000 description 2
- 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
- 102400000525 Fibrinopeptide A Human genes 0.000 description 2
- 101001027128 Homo sapiens Fibronectin Proteins 0.000 description 2
- 102000029797 Prion Human genes 0.000 description 2
- 108091000054 Prion Proteins 0.000 description 2
- 208000018756 Variant Creutzfeldt-Jakob disease Diseases 0.000 description 2
- 230000003213 activating effect Effects 0.000 description 2
- 230000002776 aggregation Effects 0.000 description 2
- 238000004220 aggregation Methods 0.000 description 2
- 230000002052 anaphylactic effect Effects 0.000 description 2
- 208000003455 anaphylaxis Diseases 0.000 description 2
- 229960004233 ancrod Drugs 0.000 description 2
- 239000000427 antigen Substances 0.000 description 2
- 230000000890 antigenic effect Effects 0.000 description 2
- 108091007433 antigens Proteins 0.000 description 2
- 102000036639 antigens Human genes 0.000 description 2
- 208000005881 bovine spongiform encephalopathy Diseases 0.000 description 2
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- QZAYGJVTTNCVMB-UHFFFAOYSA-N serotonin Chemical group C1=C(O)C=C2C(CCN)=CNC2=C1 QZAYGJVTTNCVMB-UHFFFAOYSA-N 0.000 description 2
- 238000011477 surgical intervention Methods 0.000 description 2
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- 108010050939 thrombocytin Proteins 0.000 description 2
- 230000029663 wound healing Effects 0.000 description 2
- 241000271039 Agkistrodon Species 0.000 description 1
- 241000271511 Bothrops atrox Species 0.000 description 1
- 241000271581 Calloselasma Species 0.000 description 1
- 206010053567 Coagulopathies Diseases 0.000 description 1
- 241000271037 Crotalinae Species 0.000 description 1
- 229920001651 Cyanoacrylate Polymers 0.000 description 1
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- 108010062466 Enzyme Precursors Proteins 0.000 description 1
- 102000010911 Enzyme Precursors Human genes 0.000 description 1
- 101800003778 Fibrinopeptide B Proteins 0.000 description 1
- 101000975003 Homo sapiens Kallistatin Proteins 0.000 description 1
- 101001077723 Homo sapiens Serine protease inhibitor Kazal-type 6 Proteins 0.000 description 1
- 108090000144 Human Proteins Proteins 0.000 description 1
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- 206010061218 Inflammation Diseases 0.000 description 1
- 229940122920 Kallikrein inhibitor Drugs 0.000 description 1
- 241000270322 Lepidosauria Species 0.000 description 1
- 101001017827 Mus musculus Leucine-rich repeat flightless-interacting protein 1 Proteins 0.000 description 1
- 102000013566 Plasminogen Human genes 0.000 description 1
- 108010051456 Plasminogen Proteins 0.000 description 1
- 108010094028 Prothrombin Proteins 0.000 description 1
- 102100027378 Prothrombin Human genes 0.000 description 1
- 229920002684 Sepharose Polymers 0.000 description 1
- 102100025421 Serine protease inhibitor Kazal-type 6 Human genes 0.000 description 1
- 229920002125 Sokalan® Polymers 0.000 description 1
- 101710172711 Structural protein Proteins 0.000 description 1
- 241000282887 Suidae Species 0.000 description 1
- 108090000631 Trypsin Proteins 0.000 description 1
- 102000004142 Trypsin Human genes 0.000 description 1
- 238000004026 adhesive bonding Methods 0.000 description 1
- 239000012790 adhesive layer Substances 0.000 description 1
- 235000001014 amino acid Nutrition 0.000 description 1
- 150000001413 amino acids Chemical class 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 230000001567 anti-fibrinolytic effect Effects 0.000 description 1
- 239000003146 anticoagulant agent Substances 0.000 description 1
- 229940127219 anticoagulant drug Drugs 0.000 description 1
- 239000000504 antifibrinolytic agent Substances 0.000 description 1
- 229940082620 antifibrinolytics Drugs 0.000 description 1
- 239000004019 antithrombin Substances 0.000 description 1
- 229940127217 antithrombotic drug Drugs 0.000 description 1
- 210000000709 aorta Anatomy 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
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- 230000007547 defect Effects 0.000 description 1
- 230000007123 defense Effects 0.000 description 1
- 230000003536 defibrinogenating effect Effects 0.000 description 1
- 125000002228 disulfide group Chemical group 0.000 description 1
- 229940021013 electrolyte solution Drugs 0.000 description 1
- 230000008030 elimination Effects 0.000 description 1
- 238000003379 elimination reaction Methods 0.000 description 1
- 210000002889 endothelial cell Anatomy 0.000 description 1
- 150000002148 esters Chemical class 0.000 description 1
- 230000003480 fibrinolytic effect Effects 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 238000001879 gelation Methods 0.000 description 1
- 210000004907 gland Anatomy 0.000 description 1
- 239000003292 glue Substances 0.000 description 1
- 150000004676 glycans Chemical class 0.000 description 1
- 208000006454 hepatitis Diseases 0.000 description 1
- 231100000283 hepatitis Toxicity 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
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- 239000003112 inhibitor Substances 0.000 description 1
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- 238000011835 investigation Methods 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- 230000007794 irritation Effects 0.000 description 1
- QRWOVIRDHQJFDB-UHFFFAOYSA-N isobutyl cyanoacrylate Chemical compound CC(C)COC(=O)C(=C)C#N QRWOVIRDHQJFDB-UHFFFAOYSA-N 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 238000010297 mechanical methods and process Methods 0.000 description 1
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- 239000000178 monomer Substances 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
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- 231100000614 poison Toxicity 0.000 description 1
- 239000002574 poison Substances 0.000 description 1
- 239000004584 polyacrylic acid Substances 0.000 description 1
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- 230000008569 process Effects 0.000 description 1
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- 239000012460 protein solution Substances 0.000 description 1
- 229940039716 prothrombin Drugs 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 230000035945 sensitivity Effects 0.000 description 1
- 238000009958 sewing Methods 0.000 description 1
- 210000004872 soft tissue Anatomy 0.000 description 1
- 230000000087 stabilizing effect Effects 0.000 description 1
- 239000007858 starting material Substances 0.000 description 1
- 238000011146 sterile filtration Methods 0.000 description 1
- 238000005728 strengthening Methods 0.000 description 1
- 230000001225 therapeutic effect Effects 0.000 description 1
- 229960003766 thrombin (human) Drugs 0.000 description 1
- 230000002885 thrombogenetic effect Effects 0.000 description 1
- 230000000472 traumatic effect Effects 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
- 239000012588 trypsin Substances 0.000 description 1
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- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-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
-
- 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
- A61L24/001—Use of materials characterised by their function or physical properties
- A61L24/0015—Medicaments; Biocides
-
- 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
- A61L2300/00—Biologically active materials used in bandages, wound dressings, absorbent pads or medical devices
- A61L2300/40—Biologically active materials used in bandages, wound dressings, absorbent pads or medical devices characterised by a specific therapeutic activity or mode of action
- A61L2300/418—Agents promoting blood coagulation, blood-clotting agents, embolising agents
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Surgery (AREA)
- Epidemiology (AREA)
- Animal Behavior & Ethology (AREA)
- General Health & Medical Sciences (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Materials Engineering (AREA)
- Engineering & Computer Science (AREA)
- Chemical & Material Sciences (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Materials For Medical Uses (AREA)
Priority Applications (4)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CH606/91A CH681693A5 (en, 2012) | 1991-02-28 | 1991-02-28 | |
| PCT/CH1992/000036 WO1992015341A1 (de) | 1991-02-28 | 1992-02-21 | Kleber zum verkleben von biologischen geweben |
| AU12515/92A AU1251592A (en) | 1991-02-28 | 1992-02-21 | Adhesive for bonding biological tissue |
| US08/650,027 US6613324B1 (en) | 1991-02-28 | 1996-05-17 | Adhesive for the gluing of biological tissues |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CH606/91A CH681693A5 (en, 2012) | 1991-02-28 | 1991-02-28 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CH681693A5 true CH681693A5 (en, 2012) | 1993-05-14 |
Family
ID=4190893
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CH606/91A CH681693A5 (en, 2012) | 1991-02-28 | 1991-02-28 |
Country Status (3)
| Country | Link |
|---|---|
| AU (1) | AU1251592A (en, 2012) |
| CH (1) | CH681693A5 (en, 2012) |
| WO (1) | WO1992015341A1 (en, 2012) |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2004024198A1 (en) * | 2002-09-10 | 2004-03-25 | New Dawn-Consultores E Servicos Lda | Activator for forming platelet gel, platelet poor plasma gel or platelet rich plasma gel |
Families Citing this family (10)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0534178B1 (en) * | 1991-09-27 | 2001-04-18 | Omrix Biopharmaceuticals S.A. | Improved tissue glue prepared by using cryoprecipitate |
| SK5095A3 (en) * | 1992-07-18 | 1995-07-11 | Opperbas Holding Bv | Two component fibrin-glue composition for improving in vitro fertilization |
| CN1091315A (zh) * | 1992-10-08 | 1994-08-31 | E·R·斯奎布父子公司 | 血纤维蛋白封闭剂组合物及其使用方法 |
| US6019993A (en) * | 1993-03-30 | 2000-02-01 | Omrix Biopharmaceuticals S.A. | Virus-inactivated 2-component fibrin glue |
| US6074663A (en) * | 1995-01-16 | 2000-06-13 | Baxter International Inc. | Method of using cross-linked fibrin material |
| AUPP421498A0 (en) * | 1998-06-18 | 1998-07-09 | Macquarie Research Limited | Method of tissue repair |
| BE1012536A3 (fr) | 1998-11-04 | 2000-12-05 | Baxter Int | Element muni d'une couche de fibrine sa preparation et son utilisation. |
| US7135027B2 (en) | 2002-10-04 | 2006-11-14 | Baxter International, Inc. | Devices and methods for mixing and extruding medically useful compositions |
| WO2006044879A2 (en) | 2004-10-20 | 2006-04-27 | Ethicon, Inc. | Absorbable hemostat |
| US9358318B2 (en) | 2004-10-20 | 2016-06-07 | Ethicon, Inc. | Method of making a reinforced absorbable multilayered hemostatic wound dressing |
Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE2201993A1 (de) * | 1971-01-18 | 1972-08-10 | Pentapharm Ag | Enzympraeparat und Verfahren zu dessen Herstellung |
-
1991
- 1991-02-28 CH CH606/91A patent/CH681693A5/de not_active IP Right Cessation
-
1992
- 1992-02-21 AU AU12515/92A patent/AU1251592A/en not_active Abandoned
- 1992-02-21 WO PCT/CH1992/000036 patent/WO1992015341A1/de unknown
Patent Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE2201993A1 (de) * | 1971-01-18 | 1972-08-10 | Pentapharm Ag | Enzympraeparat und Verfahren zu dessen Herstellung |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2004024198A1 (en) * | 2002-09-10 | 2004-03-25 | New Dawn-Consultores E Servicos Lda | Activator for forming platelet gel, platelet poor plasma gel or platelet rich plasma gel |
Also Published As
| Publication number | Publication date |
|---|---|
| AU1251592A (en) | 1992-10-06 |
| WO1992015341A1 (de) | 1992-09-17 |
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| Date | Code | Title | Description |
|---|---|---|---|
| PUE | Assignment |
Owner name: PENTAPHARM AG TRANSFER- E.R. SQUIBB & SONS, INC. * |
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| PL | Patent ceased |