CH681693A5 - - Google Patents

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Info

Publication number: CH681693A5
Authority: CH; Switzerland
Prior art keywords: adhesive; fibrinogen; adhesive according; enzyme; batroxobin
Prior art date: 1991-02-28

Application number

CH606/91A

Other languages

German (de)

English (en)

Inventor

Birger Blombaeck

Birgit Hessel

Per Olsson

Lennart Stroemberg

Jesper Swedenborg

Kurt Stocker

Original Assignee

Pentapharm 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.)

1991-02-28

Filing date

1991-02-28

Publication date

1993-05-14

1991-02-28 Application filed by Pentapharm Ag filed Critical Pentapharm Ag

1991-02-28 Priority to CH606/91A priority Critical patent/CH681693A5/de

1992-02-21 Priority to AU12515/92A priority patent/AU1251592A/en

1992-02-21 Priority to PCT/CH1992/000036 priority patent/WO1992015341A1/fr

1993-05-14 Publication of CH681693A5 publication Critical patent/CH681693A5/de

1996-05-17 Priority to US08/650,027 priority patent/US6613324B1/en

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
239000000872 buffer Substances 0.000 description 2
230000015271 coagulation Effects 0.000 description 2
238000005345 coagulation Methods 0.000 description 2
238000004090 dissolution Methods 0.000 description 2
239000003814 drug Substances 0.000 description 2
239000004744 fabric Substances 0.000 description 2
238000004519 manufacturing process Methods 0.000 description 2
239000012528 membrane Substances 0.000 description 2
230000001717 pathogenic effect Effects 0.000 description 2
239000011541 reaction mixture Substances 0.000 description 2
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
230000002345 thrombinlike Effects 0.000 description 2
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
206010014523 Embolism and thrombosis Diseases 0.000 description 1
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
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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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239000007853 buffer solution Substances 0.000 description 1
238000005119 centrifugation Methods 0.000 description 1
239000003795 chemical substances by application Substances 0.000 description 1
238000007705 chemical test Methods 0.000 description 1
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230000035602 clotting Effects 0.000 description 1
239000013065 commercial product Substances 0.000 description 1
150000001875 compounds Chemical class 0.000 description 1
238000011109 contamination Methods 0.000 description 1
229920001577 copolymer Polymers 0.000 description 1
238000004132 cross linking Methods 0.000 description 1
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
230000002779 inactivation Effects 0.000 description 1
230000004054 inflammatory process Effects 0.000 description 1
239000003112 inhibitor Substances 0.000 description 1
230000002401 inhibitory effect Effects 0.000 description 1
238000002347 injection Methods 0.000 description 1
239000007924 injection Substances 0.000 description 1
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
230000005226 mechanical processes and functions Effects 0.000 description 1
239000000178 monomer Substances 0.000 description 1
210000000056 organ Anatomy 0.000 description 1
235000011837 pasties Nutrition 0.000 description 1
230000001575 pathological effect Effects 0.000 description 1
230000035699 permeability Effects 0.000 description 1
238000000053 physical method Methods 0.000 description 1
231100000614 poison Toxicity 0.000 description 1
239000002574 poison Substances 0.000 description 1
239000004584 polyacrylic acid Substances 0.000 description 1
229920000642 polymer Polymers 0.000 description 1
229920001282 polysaccharide Polymers 0.000 description 1
239000005017 polysaccharide Substances 0.000 description 1
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239000012460 protein solution Substances 0.000 description 1
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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
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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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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)

CH606/91A 1991-02-28 1991-02-28 CH681693A5 (fr)

Priority Applications (4)

Application Number	Priority Date	Filing Date	Title
CH606/91A CH681693A5 (fr)	1991-02-28	1991-02-28
AU12515/92A AU1251592A (en)	1991-02-28	1992-02-21	Adhesive for bonding biological tissue
PCT/CH1992/000036 WO1992015341A1 (fr)	1991-02-28	1992-02-21	Colle pour le collage de tissus biologiques
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 (fr)	1991-02-28	1991-02-28

Publications (1)

Publication Number	Publication Date
CH681693A5 true CH681693A5 (fr)	1993-05-14

Family

ID=4190893

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
CH606/91A CH681693A5 (fr)	1991-02-28	1991-02-28

Country Status (3)

Country	Link
AU (1)	AU1251592A (fr)
CH (1)	CH681693A5 (fr)
WO (1)	WO1992015341A1 (fr)

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
WO2004024198A1 (fr) *	2002-09-10	2004-03-25	New Dawn-Consultores E Servicos Lda	Activateur utilise pour former un gel plaquettaire, un gel de plasma pauvre en plaquettes ou un gel de plasma riche en plaquettes

Families Citing this family (10)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
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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
ATE187651T1 (de) *	1993-03-30	2000-01-15	Omrix Biopharm Sa	Zweikomponenten-fibrinkleber
CA2207992A1 (fr) *	1995-01-16	1996-07-25	Genevieve Krack	Materiau du type feuille autonome compose de fibrine reticulee, destine a prevenir les adherences postoperatoires
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
US9358318B2 (en)	2004-10-20	2016-06-07	Ethicon, Inc.	Method of making a reinforced absorbable multilayered hemostatic wound dressing
EP1809343B1 (fr)	2004-10-20	2012-08-15	Ethicon, Inc.	Pansement hemostatique multicouche absorbable renforce et son procede de fabrication

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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 WO PCT/CH1992/000036 patent/WO1992015341A1/fr not_active Ceased
- 1992-02-21 AU AU12515/92A patent/AU1251592A/en not_active Abandoned

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Cited By (1)

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Publication number	Priority date	Publication date	Assignee	Title
WO2004024198A1 (fr) *	2002-09-10	2004-03-25	New Dawn-Consultores E Servicos Lda	Activateur utilise pour former un gel plaquettaire, un gel de plasma pauvre en plaquettes ou un gel de plasma riche en plaquettes

Also Published As

Publication number	Publication date
AU1251592A (en)	1992-10-06
WO1992015341A1 (fr)	1992-09-17

Legal Events

Date	Code	Title	Description
1998-02-27	PUE	Assignment	Owner name: PENTAPHARM AG TRANSFER- E.R. SQUIBB & SONS, INC. *
2010-09-30	PL	Patent ceased

Publication	Publication Date	Title
Hanson et al.	2020	Blood coagulation and blood–material interactions
US6056970A (en)	2000-05-02	Compositions comprising hemostatic compounds and bioabsorbable polymers
US5290552A (en)	1994-03-01	Surgical adhesive material
AU2004206150B2 (en)	2009-10-29	Hemostatic materials
DE69433939T2 (de)	2005-08-11	Hämostatisches pflaster
DE19521324C1 (de)	1996-10-31	Gewebeklebstoff und Verwendung desselben als Hämostyptikum
KRAM et al.	1988	Use of fibrin glue in hepatic trauma
CA2131316C (fr)	2002-03-19	Fraction thrombine du sang pour utilisation dans une procedure medicale
US5298255A (en)	1994-03-29	Antithrombic medical material, artificial internal organ, and method for production of antithrombic medical material
US20050118156A1 (en)	2005-06-02	Storage-stable fibrin sealant
DE68923423T2 (de)	1996-01-25	Antithromotisches medizinisches Material, künstliches inneres Organ und Verfahren zur Herstellung eines antithrombotischen medizinischen Materials.
JPH02129224A (ja)	1990-05-17	フィブリンの製造法
CH681693A5 (fr)	1993-05-14
Jackson et al.	1999	Hemostatic efficacy of fibrin sealant (human) on expanded poly-tetrafluoroethylene carotid patch angioplasty: a randomized clinical trial
US6613324B1 (en)	2003-09-02	Adhesive for the gluing of biological tissues
AU2003280730B2 (en)	2010-04-29	Thrombin-carrying bioabsorbable synthetic nonwoven fabric
Jakob et al.	1984	Use of fibrin sealant for reinforcing arterial anastomoses
EP1528930B1 (fr)	2009-04-15	Preparations pharmaceutiques de substances actives a capacite de production de thrombine et contenant de la thrombine et medicaments
RU2198684C2 (ru)	2003-02-20	Гемостатическая губка и способ ее получения
EP1523327A1 (fr)	2005-04-20	Preparations de principes actifs pharmaceutiques et medicaments generant ou contenant de la thrombine
Peper et al.	1986	Pigskin as a topical hemostat in arterial, liver, and splenic injuries
US6946140B1 (en)	2005-09-20	Methods and compositions for enhancing fibroblast migration
UA129819C2 (uk)	2025-08-06	Комплект для оптимізованого одержання аутологічного фібринового гелю ех tempore для використання в хірургії
UA128188C2 (uk)	2024-05-01	Спосіб надання біоматеріалам прокоагулянтних властивостей шляхом модифікації їхньої поверхні екзогенним активатором протромбіну екамуліном
Duda et al.	1993	Testing method for mechanical properties of fibrin glue

CH681693A5 - - Google Patents

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