CA1217134A - Proteolytic cover of wounds - Google Patents

Proteolytic cover of wounds

Info

Publication number: CA1217134A
Authority: CA; Canada
Prior art keywords: cellulose; proteolytic; wounds; cover; buffer
Prior art date: 1983-09-29
Legal status (The legal status 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 status listed.): Expired

Application number

CA000464332A

Other languages

English (en)

French (fr)

Inventor

Jaroslava Turkova

Jiri Stamberg

Vladimir Pitrak

Lenka Jelinkova

Karel Sebesta

Mojmir Sebestik

Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)

Czech Academy of Sciences CAS

Original Assignee

Czech Academy of Sciences CAS

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.)

1983-09-29

Filing date

1984-09-28

Publication date

1987-01-27

1984-09-28 Application filed by Czech Academy of Sciences CAS filed Critical Czech Academy of Sciences CAS

1987-01-27 Application granted granted Critical

1987-01-27 Publication of CA1217134A publication Critical patent/CA1217134A/en

Status Expired legal-status Critical Current

Links

206010052428 Wound Diseases 0.000 title claims abstract description 43
208000027418 Wounds and injury Diseases 0.000 title claims abstract description 43
230000002797 proteolythic effect Effects 0.000 title claims abstract description 37
239000001913 cellulose Substances 0.000 claims abstract description 51
229920002678 cellulose Polymers 0.000 claims abstract description 50
108091005804 Peptidases Proteins 0.000 claims abstract description 17
239000004365 Protease Substances 0.000 claims abstract description 17
238000000034 method Methods 0.000 claims abstract description 13
239000002245 particle Substances 0.000 claims abstract description 12
102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims abstract description 10
238000004519 manufacturing process Methods 0.000 claims abstract description 9
108010093096 Immobilized Enzymes Proteins 0.000 claims abstract description 8
239000012798 spherical particle Substances 0.000 claims abstract description 7
239000000872 buffer Substances 0.000 claims description 18
239000000203 mixture Substances 0.000 claims description 15
102000004190 Enzymes Human genes 0.000 claims description 14
108090000790 Enzymes Proteins 0.000 claims description 14
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 13
230000027455 binding Effects 0.000 claims description 11
238000009739 binding Methods 0.000 claims description 11
239000011324 bead Substances 0.000 claims description 10
238000005406 washing Methods 0.000 claims description 8
102000035195 Peptidases Human genes 0.000 claims description 7
231100000331 toxic Toxicity 0.000 claims description 6
230000002588 toxic effect Effects 0.000 claims description 6
238000004821 distillation Methods 0.000 claims description 5
238000004108 freeze drying Methods 0.000 claims description 4
239000012535 impurity Substances 0.000 claims description 4
239000000126 substance Substances 0.000 claims description 4
239000007788 liquid Substances 0.000 claims description 3
239000004627 regenerated cellulose Substances 0.000 claims 2
230000007547 defect Effects 0.000 abstract description 28
238000005469 granulation Methods 0.000 abstract description 14
230000003179 granulation Effects 0.000 abstract description 14
230000001338 necrotic effect Effects 0.000 abstract description 13
239000000843 powder Substances 0.000 abstract description 12
238000010521 absorption reaction Methods 0.000 abstract description 11
238000004140 cleaning Methods 0.000 abstract description 10
238000011282 treatment Methods 0.000 abstract description 8
230000035876 healing Effects 0.000 abstract description 6
241000894006 Bacteria Species 0.000 abstract description 5
239000000427 antigen Substances 0.000 abstract description 5
108091007433 antigens Proteins 0.000 abstract description 5
102000036639 antigens Human genes 0.000 abstract description 5
230000017531 blood circulation Effects 0.000 abstract description 5
102000004169 proteins and genes Human genes 0.000 abstract description 5
108090000623 proteins and genes Proteins 0.000 abstract description 5
210000000416 exudates and transudate Anatomy 0.000 abstract description 4
102000009123 Fibrin Human genes 0.000 abstract description 3
108010073385 Fibrin Proteins 0.000 abstract description 3
BWGVNKXGVNDBDI-UHFFFAOYSA-N Fibrin monomer Chemical compound CNC(=O)CNC(=O)CN BWGVNKXGVNDBDI-UHFFFAOYSA-N 0.000 abstract description 3
230000015572 biosynthetic process Effects 0.000 abstract description 3
238000006243 chemical reaction Methods 0.000 abstract description 3
229950003499 fibrin Drugs 0.000 abstract description 3
238000001179 sorption measurement Methods 0.000 abstract description 3
239000000463 material Substances 0.000 abstract description 2
231100000167 toxic agent Toxicity 0.000 abstract description 2
235000010980 cellulose Nutrition 0.000 description 36
238000002360 preparation method Methods 0.000 description 24
230000028327 secretion Effects 0.000 description 14
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 10
230000009102 absorption Effects 0.000 description 8
238000002266 amputation Methods 0.000 description 8
230000009467 reduction Effects 0.000 description 8
239000000243 solution Substances 0.000 description 8
206010012665 Diabetic gangrene Diseases 0.000 description 7
BTBUEUYNUDRHOZ-UHFFFAOYSA-N Borate Chemical compound [O-]B([O-])[O-] BTBUEUYNUDRHOZ-UHFFFAOYSA-N 0.000 description 6
230000000694 effects Effects 0.000 description 6
230000003647 oxidation Effects 0.000 description 5
238000007254 oxidation reaction Methods 0.000 description 5
239000011780 sodium chloride Substances 0.000 description 5
210000003371 toe Anatomy 0.000 description 5
206010007882 Cellulitis Diseases 0.000 description 4
208000033809 Suppuration Diseases 0.000 description 4
MVPPADPHJFYWMZ-UHFFFAOYSA-N chlorobenzene Chemical compound ClC1=CC=CC=C1 MVPPADPHJFYWMZ-UHFFFAOYSA-N 0.000 description 4
239000012153 distilled water Substances 0.000 description 4
JQWHASGSAFIOCM-UHFFFAOYSA-M sodium periodate Chemical compound [Na+].[O-]I(=O)(=O)=O JQWHASGSAFIOCM-UHFFFAOYSA-M 0.000 description 4
239000008280 blood Substances 0.000 description 3
210000004369 blood Anatomy 0.000 description 3
206010003210 Arteriosclerosis Diseases 0.000 description 2
241000725101 Clea Species 0.000 description 2
206010054044 Diabetic microangiopathy Diseases 0.000 description 2
LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 2
229920002201 Oxidized cellulose Polymers 0.000 description 2
208000025865 Ulcer Diseases 0.000 description 2
230000004913 activation Effects 0.000 description 2
125000003172 aldehyde group Chemical group 0.000 description 2
150000001413 amino acids Chemical class 0.000 description 2
210000003447 amputation stump Anatomy 0.000 description 2
208000011775 arteriosclerosis disease Diseases 0.000 description 2
230000001580 bacterial effect Effects 0.000 description 2
239000002585 base Substances 0.000 description 2
230000036770 blood supply Effects 0.000 description 2
230000000052 comparative effect Effects 0.000 description 2
150000001875 compounds Chemical class 0.000 description 2
238000000354 decomposition reaction Methods 0.000 description 2
230000003247 decreasing effect Effects 0.000 description 2
201000009101 diabetic angiopathy Diseases 0.000 description 2
238000001035 drying Methods 0.000 description 2
230000002255 enzymatic effect Effects 0.000 description 2
230000000670 limiting effect Effects 0.000 description 2
229940107304 oxidized cellulose Drugs 0.000 description 2
230000035515 penetration Effects 0.000 description 2
KHIWWQKSHDUIBK-UHFFFAOYSA-N periodic acid Chemical compound OI(=O)(=O)=O KHIWWQKSHDUIBK-UHFFFAOYSA-N 0.000 description 2
230000008569 process Effects 0.000 description 2
230000002829 reductive effect Effects 0.000 description 2
229910000033 sodium borohydride Inorganic materials 0.000 description 2
239000012279 sodium borohydride Substances 0.000 description 2
238000005063 solubilization Methods 0.000 description 2
230000007928 solubilization Effects 0.000 description 2
239000007858 starting material Substances 0.000 description 2
231100000397 ulcer Toxicity 0.000 description 2
QTBSBXVTEAMEQO-UHFFFAOYSA-M Acetate Chemical compound CC([O-])=O QTBSBXVTEAMEQO-UHFFFAOYSA-M 0.000 description 1
239000004475 Arginine Substances 0.000 description 1
229920002134 Carboxymethyl cellulose Polymers 0.000 description 1
206010007247 Carbuncle Diseases 0.000 description 1
QDHHCQZDFGDHMP-UHFFFAOYSA-N Chloramine Chemical compound ClN QDHHCQZDFGDHMP-UHFFFAOYSA-N 0.000 description 1
241000272470 Circus Species 0.000 description 1
SNPLKNRPJHDVJA-ZETCQYMHSA-N D-panthenol Chemical compound OCC(C)(C)[C@@H](O)C(=O)NCCCO SNPLKNRPJHDVJA-ZETCQYMHSA-N 0.000 description 1
YZCKVEUIGOORGS-OUBTZVSYSA-N Deuterium Chemical compound [2H] YZCKVEUIGOORGS-OUBTZVSYSA-N 0.000 description 1
229920002307 Dextran Polymers 0.000 description 1
ZNZYKNKBJPZETN-WELNAUFTSA-N Dialdehyde 11678 Chemical group N1C2=CC=CC=C2C2=C1[C@H](C[C@H](/C(=C/O)C(=O)OC)[C@@H](C=C)C=O)NCC2 ZNZYKNKBJPZETN-WELNAUFTSA-N 0.000 description 1
206010017711 Gangrene Diseases 0.000 description 1
MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 1
DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
206010061218 Inflammation Diseases 0.000 description 1
239000004472 Lysine Substances 0.000 description 1
KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 1
206010028980 Neoplasm Diseases 0.000 description 1
208000002565 Open Fractures Diseases 0.000 description 1
239000002262 Schiff base Substances 0.000 description 1
150000004753 Schiff bases Chemical class 0.000 description 1
229920002472 Starch Polymers 0.000 description 1
208000002847 Surgical Wound Diseases 0.000 description 1
239000008351 acetate buffer Substances 0.000 description 1
230000002378 acidificating effect Effects 0.000 description 1
230000009471 action Effects 0.000 description 1
239000000654 additive Substances 0.000 description 1
230000000996 additive effect Effects 0.000 description 1
150000001299 aldehydes Chemical class 0.000 description 1
239000003242 anti bacterial agent Substances 0.000 description 1
230000000844 anti-bacterial effect Effects 0.000 description 1
230000001857 anti-mycotic effect Effects 0.000 description 1
229940088710 antibiotic agent Drugs 0.000 description 1
239000002543 antimycotic Substances 0.000 description 1
ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
210000001367 artery Anatomy 0.000 description 1
239000003899 bactericide agent Substances 0.000 description 1
239000000022 bacteriostatic agent Substances 0.000 description 1
230000003385 bacteriostatic effect Effects 0.000 description 1
230000008901 benefit Effects 0.000 description 1
239000001768 carboxy methyl cellulose Substances 0.000 description 1
235000010948 carboxy methyl cellulose Nutrition 0.000 description 1
239000008112 carboxymethyl-cellulose Substances 0.000 description 1
229940105329 carboxymethylcellulose Drugs 0.000 description 1
229940106135 cellulose Drugs 0.000 description 1
230000001684 chronic effect Effects 0.000 description 1
239000011248 coating agent Substances 0.000 description 1
238000000576 coating method Methods 0.000 description 1
239000000356 contaminant Substances 0.000 description 1
206010012601 diabetes mellitus Diseases 0.000 description 1
238000004090 dissolution Methods 0.000 description 1
238000009826 distribution Methods 0.000 description 1
239000003814 drug Substances 0.000 description 1
239000000428 dust Substances 0.000 description 1
238000010828 elution Methods 0.000 description 1
238000002474 experimental method Methods 0.000 description 1
239000008187 granular material Substances 0.000 description 1
229960000789 guanidine hydrochloride Drugs 0.000 description 1
PJJJBBJSCAKJQF-UHFFFAOYSA-N guanidinium chloride Chemical compound [Cl-].NC(N)=[NH2+] PJJJBBJSCAKJQF-UHFFFAOYSA-N 0.000 description 1
238000010438 heat treatment Methods 0.000 description 1
230000003301 hydrolyzing effect Effects 0.000 description 1
229920001477 hydrophilic polymer Polymers 0.000 description 1
230000002209 hydrophobic effect Effects 0.000 description 1
230000004054 inflammatory process Effects 0.000 description 1
230000003993 interaction Effects 0.000 description 1
238000005342 ion exchange Methods 0.000 description 1
150000002500 ions Chemical class 0.000 description 1
208000028867 ischemia Diseases 0.000 description 1
238000002803 maceration Methods 0.000 description 1
239000011159 matrix material Substances 0.000 description 1
235000015097 nutrients Nutrition 0.000 description 1
229940101267 panthenol Drugs 0.000 description 1
235000020957 pantothenol Nutrition 0.000 description 1
239000011619 pantothenol Substances 0.000 description 1
230000002093 peripheral effect Effects 0.000 description 1
229920000642 polymer Polymers 0.000 description 1
239000011148 porous material Substances 0.000 description 1
230000000750 progressive effect Effects 0.000 description 1
230000002035 prolonged effect Effects 0.000 description 1
230000000717 retained effect Effects 0.000 description 1
229910052708 sodium Inorganic materials 0.000 description 1
239000011734 sodium Substances 0.000 description 1
239000007921 spray Substances 0.000 description 1
230000007480 spreading Effects 0.000 description 1
238000003892 spreading Methods 0.000 description 1
239000008107 starch Substances 0.000 description 1
235000019698 starch Nutrition 0.000 description 1
230000003068 static effect Effects 0.000 description 1
238000003756 stirring Methods 0.000 description 1
229940124530 sulfonamide Drugs 0.000 description 1
150000003456 sulfonamides Chemical class 0.000 description 1
230000001629 suppression Effects 0.000 description 1
239000000725 suspension Substances 0.000 description 1
239000000454 talc Substances 0.000 description 1
229910052623 talc Inorganic materials 0.000 description 1
239000003053 toxin Substances 0.000 description 1
231100000765 toxin Toxicity 0.000 description 1
108700012359 toxins Proteins 0.000 description 1
230000001228 trophic 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
- C12N11/00—Carrier-bound or immobilised enzymes; Carrier-bound or immobilised microbial cells; Preparation thereof
- C12N11/02—Enzymes or microbial cells immobilised on or in an organic carrier
- C12N11/10—Enzymes or microbial cells immobilised on or in an organic carrier the carrier being a carbohydrate
- C12N11/12—Cellulose or derivatives thereof
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/43—Enzymes; Proenzymes; Derivatives thereof
- A61K38/46—Hydrolases (3)
- A61K38/48—Hydrolases (3) acting on peptide bonds (3.4)
- A61K38/482—Serine endopeptidases (3.4.21)
- A61K38/4826—Trypsin (3.4.21.4) Chymotrypsin (3.4.21.1)
- 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
- A61L26/00—Chemical aspects of, or use of materials for, wound dressings or bandages in liquid, gel or powder form
- A61L26/0009—Chemical aspects of, or use of materials for, wound dressings or bandages in liquid, gel or powder form containing macromolecular materials
- A61L26/0023—Polysaccharides
- 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
- A61L26/00—Chemical aspects of, or use of materials for, wound dressings or bandages in liquid, gel or powder form
- A61L26/0057—Ingredients of undetermined constitution or reaction products thereof
- 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
- A61L26/00—Chemical aspects of, or use of materials for, wound dressings or bandages in liquid, gel or powder form
- A61L26/0061—Use of materials characterised by their function or physical properties
- A61L26/0066—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
- A61L2300/20—Biologically active materials used in bandages, wound dressings, absorbent pads or medical devices containing or releasing organic materials
- A61L2300/252—Polypeptides, proteins, e.g. glycoproteins, lipoproteins, cytokines
- A61L2300/254—Enzymes, proenzymes

Landscapes

Health & Medical Sciences (AREA)
Life Sciences & Earth Sciences (AREA)
Chemical & Material Sciences (AREA)
Engineering & Computer Science (AREA)
General Health & Medical Sciences (AREA)
Public Health (AREA)
Epidemiology (AREA)
Animal Behavior & Ethology (AREA)
Veterinary Medicine (AREA)
Materials Engineering (AREA)
Bioinformatics & Cheminformatics (AREA)
Genetics & Genomics (AREA)
Zoology (AREA)
Wood Science & Technology (AREA)
Organic Chemistry (AREA)
Microbiology (AREA)
Medicinal Chemistry (AREA)
Biomedical Technology (AREA)
Molecular Biology (AREA)
Biochemistry (AREA)
General Engineering & Computer Science (AREA)
Chemical Kinetics & Catalysis (AREA)
Gastroenterology & Hepatology (AREA)
Immunology (AREA)
Biotechnology (AREA)
Pharmacology & Pharmacy (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Medicinal Preparation (AREA)
Medicines Containing Material From Animals Or Micro-Organisms (AREA)
Immobilizing And Processing Of Enzymes And Microorganisms (AREA)
Materials For Medical Uses (AREA)

CA000464332A 1983-09-29 1984-09-28 Proteolytic cover of wounds Expired CA1217134A (en)

Applications Claiming Priority (2)

Application Number	Priority Date	Filing Date	Title
CSPV7138-83		1983-09-29
CS713883A CS249311B1 (en)	1983-09-29	1983-09-29	Proteolytic wound dressing

Publications (1)

Publication Number	Publication Date
CA1217134A true CA1217134A (en)	1987-01-27

Family

ID=5419947

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
CA000464332A Expired CA1217134A (en)	1983-09-29	1984-09-28	Proteolytic cover of wounds

Country Status (9)

Country	Link
JP (1)	JPS6094916A (cs)
CA (1)	CA1217134A (cs)
CS (1)	CS249311B1 (cs)
DD (1)	DD258121A3 (cs)
DE (1)	DE3435718A1 (cs)
FR (1)	FR2552667B1 (cs)
GB (1)	GB2147206B (cs)
HU (1)	HUT35956A (cs)
SE (1)	SE8404769L (cs)

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
EP2279762A1 (en)	2009-07-30	2011-02-02	Franzoni Filati S.p.A.	Pregelatinized aminoglycosides covalently conjugated to cotton

Families Citing this family (14)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
DE3606265A1 (de) *	1986-02-27	1987-09-03	Roehm Pharma Gmbh	Wundauflage auf polysaccharidbasis als traeger therapeutisch wirksamer, nicht-immobilisierter enzyme und mit hoher saugfaehigkeit
FR2600897A1 (fr) *	1986-07-04	1988-01-08	Pf Medicament	Pansement proteolytique et absorbant et procede pour sa preparation
CZ277766B6 (en) *	1990-01-04	1993-04-14	Vnii Textilno	Biologically active material and process for preparing thereof
EP0498532A1 (en) *	1991-01-10	1992-08-12	E.R. SQUIBB & SONS, INC.	Necrotic tissue debridement powder composition containing a proteolytic enzyme
IL104734A0 (en) *	1993-02-15	1993-06-10	Univ Bar Ilan	Bioactive conjugates of cellulose with amino compounds
DE19813663A1 (de) *	1998-03-27	1999-10-07	Beiersdorf Ag	Wundauflagen zur Entfernung von Störfaktoren aus Wundflüssigkeit
US6600057B2 (en)	2000-12-29	2003-07-29	Kimberly-Clark Worldwide, Inc.	Matrix metalloproteinase inhibitors
US7041787B2 (en)	2000-12-29	2006-05-09	Kimberly-Clark Worldwide, Inc.	Design and use of advanced zinc chelating peptides to regulate matrix metalloproteinases
RU2213557C2 (ru) *	2001-12-26	2003-10-10	Закрытое акционерное общество "Аксис"	Фармацевтическая композиция, обладающая тромболитическими, противовоспалительными и цитопротективными свойствами
EP1471935A2 (de) *	2002-02-06	2004-11-03	N-Zyme BioTec GmbH	Protease-screening und neue verwendung von proteasen
US20030198631A1 (en) *	2002-04-18	2003-10-23	Healthpoint, Ltd.	Thermolysin enzymatic wound debrider
US7928282B2 (en)	2004-04-30	2011-04-19	Kimberly-Clark Worldwide, Inc.	Absorbent products with a linked enzyme treatment
CA2890757C (en)	2012-11-14	2021-10-26	Smith & Nephew, Inc.	Stable thermolysin hydrogel
RU2015137174A (ru)	2013-03-15	2017-04-24	Смит энд Невью, Инк.	Растворимая образующая гель плёнка и способ очистки раны

Family Cites Families (3)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
RO57973A (cs) *	1969-06-13	1975-03-15
DE1938189A1 (de) *	1969-07-28	1971-02-25	Blendax Werke Schneider Co	Enzymhaltige Zahn- und Mundpflegemittel
FR2488797A1 (fr) *	1980-08-19	1982-02-26	Lhd Lab Hygiene Dietetique	Composition dermatologique, son procede de preparation et son application dans le domaine des pansements

1983
- 1983-09-29 CS CS713883A patent/CS249311B1/cs unknown
1984
- 1984-09-21 GB GB08423913A patent/GB2147206B/en not_active Expired
- 1984-09-24 SE SE8404769A patent/SE8404769L/xx not_active Application Discontinuation
- 1984-09-25 DD DD26764384A patent/DD258121A3/xx not_active IP Right Cessation
- 1984-09-28 DE DE19843435718 patent/DE3435718A1/de not_active Withdrawn
- 1984-09-28 JP JP59202175A patent/JPS6094916A/ja active Pending
- 1984-09-28 HU HU369184A patent/HUT35956A/hu unknown
- 1984-09-28 FR FR8414969A patent/FR2552667B1/fr not_active Expired
- 1984-09-28 CA CA000464332A patent/CA1217134A/en not_active Expired

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
EP2279762A1 (en)	2009-07-30	2011-02-02	Franzoni Filati S.p.A.	Pregelatinized aminoglycosides covalently conjugated to cotton

Also Published As

Publication number	Publication date
SE8404769L (sv)	1985-03-30
JPS6094916A (ja)	1985-05-28
DD258121A3 (de)	1988-07-13
HUT35956A (en)	1985-08-28
FR2552667B1 (fr)	1987-11-27
GB2147206B (en)	1988-01-27
FR2552667A1 (fr)	1985-04-05
GB8423913D0 (en)	1984-10-31
CS249311B1 (en)	1987-03-12
GB2147206A (en)	1985-05-09
SE8404769D0 (sv)	1984-09-24
DE3435718A1 (de)	1985-04-11

Legal Events

Date	Code	Title	Description
2004-09-28	MKEX	Expiry

Publication	Publication Date	Title
US4613502A (en)	1986-09-23	Proteolytic, dry biopolymeric composition for treatment of wounds, and method of using same
GB2147206A (en)	1985-05-09	Proteolytic enzyme treatment of wounds
ES2686524T3 (es)	2018-10-18	Partículas de poliacrilato y su uso
EP0611573A2 (en)	1994-08-24	Bioactive conjugates of cellulose with amino compounds
RU2619351C1 (ru)	2017-05-15	Композиция для обработки ран
JPH02218616A (ja)	1990-08-31	コラーゲン・ペースト組成物
Edwards et al.	2016	Protease biosensors based on peptide-nanocellulose conjugates: From molecular design to dressing interface
CA2429664A1 (en)	2002-07-04	Removal of targeted proteases with proteinaceous wound dressings containing growth factors
CN1197631C (zh)	2005-04-20	一种含有表皮生长因子的皮肤组织工程支架的构建方法
CN103030831B (zh)	2014-06-25	胶原止血或抗凝材料
CA2260324A1 (en)	1998-01-22	Method for preparing bioactive polymers
JPS621731B2 (cs)	1987-01-14
PITRÁK	2026	Academy of Sciences, 162 06 Prague 6, Czechoslovakia
Stamberg et al.	2026	Spherical Cellulose with Controlled Porosity for Biomedical Interactions
CS245160B1 (cs)	1986-08-14	Proteolytický kryt na rány
RU2145874C1 (ru)	2000-02-27	Способ получения некрэктомирующей повязки
SU979508A1 (ru)	1982-12-07	Способ получени иммобилизованного плазминогена
RU2323748C2 (ru)	2008-05-10	Медицинская повязка, содержащая комплекс ферментов из гепатопанкреаса краба, и способ ее получения
Jaiswar et al.	2022	1Department of Chemistry, Dr. Bhimrao Ambedkar University, Agra, India, 2Department of Chemistry, IET, Dr. Bhimrao Ambedkar University, Agra, India
CN121648340A (zh)	2026-03-13	一种自交联内脏止血粉及其制备方法和应用
WO2002051455A2 (en)	2002-07-04	Removal of targeted proteases with proteinaceous wound dressings
KR20220150776A (ko)	2022-11-11	혈액 응고 활성을 갖는 펩타이드와 이의 용도
Wang et al.	2005	Strategies for improving the functionality of an affinity bioreactor
WO1996015236A1 (en)	1996-05-23	Bioactive conjugates of polyhydroxy-polymers with amines
JPS6248630A (ja)	1987-03-03	ヘパリン含有イオン複合体

CA1217134A - Proteolytic cover of wounds - Google Patents

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