JPS6094916A - 蛋白質分解性被覆物及びその製造方法 - Google Patents

蛋白質分解性被覆物及びその製造方法

Info

Publication number: JPS6094916A
Authority: JP; Japan
Prior art keywords: cellulose; chymotrypsin; proteolytic; trypsin; defect
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.): Pending

Application number

JP59202175A

Other languages

English (en)

Japanese (ja)

Inventor

ヤロスラバ　ツルコバ

イシー　シユタンベルク

ブラデイミール　ピトラーク

レンカ　イエリンコバ

カレル　シエベスタ

モイミール　シエベステイーク

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

1985-05-28

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

1985-05-28 Publication of JPS6094916A publication Critical patent/JPS6094916A/ja

Status Pending legal-status Critical Current

Links

230000002797 proteolythic effect Effects 0.000 title claims description 15
238000004519 manufacturing process Methods 0.000 title claims description 7
238000000576 coating method Methods 0.000 title description 17
239000011248 coating agent Substances 0.000 title description 10
239000001913 cellulose Substances 0.000 claims description 38
229920002678 cellulose Polymers 0.000 claims description 38
108091005804 Peptidases Proteins 0.000 claims description 22
108090000317 Chymotrypsin Proteins 0.000 claims description 21
239000004365 Protease Substances 0.000 claims description 21
229960002376 chymotrypsin Drugs 0.000 claims description 21
102000004190 Enzymes Human genes 0.000 claims description 15
108090000790 Enzymes Proteins 0.000 claims description 15
229940088598 enzyme Drugs 0.000 claims description 15
238000000034 method Methods 0.000 claims description 13
239000000243 solution Substances 0.000 claims description 12
108090000631 Trypsin Proteins 0.000 claims description 11
102000004142 Trypsin Human genes 0.000 claims description 11
239000012588 trypsin Substances 0.000 claims description 11
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 8
239000002245 particle Substances 0.000 claims description 7
108090000787 Subtilisin Proteins 0.000 claims description 6
239000007853 buffer solution Substances 0.000 claims description 6
238000005406 washing Methods 0.000 claims description 6
108010093096 Immobilized Enzymes Proteins 0.000 claims description 5
238000004821 distillation Methods 0.000 claims description 4
238000001035 drying Methods 0.000 claims description 3
239000012798 spherical particle Substances 0.000 claims description 3
102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims 3
238000002791 soaking Methods 0.000 claims 1
206010052428 Wound Diseases 0.000 description 27
208000027418 Wounds and injury Diseases 0.000 description 27
230000007547 defect Effects 0.000 description 23
102000035195 Peptidases Human genes 0.000 description 19
230000000694 effects Effects 0.000 description 16
238000002360 preparation method Methods 0.000 description 16
239000000872 buffer Substances 0.000 description 14
238000005469 granulation Methods 0.000 description 14
230000003179 granulation Effects 0.000 description 14
230000028327 secretion Effects 0.000 description 14
206010028851 Necrosis Diseases 0.000 description 12
230000017074 necrotic cell death Effects 0.000 description 12
235000019419 proteases Nutrition 0.000 description 12
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 10
238000010521 absorption reaction Methods 0.000 description 8
BTBUEUYNUDRHOZ-UHFFFAOYSA-N Borate Chemical compound [O-]B([O-])[O-] BTBUEUYNUDRHOZ-UHFFFAOYSA-N 0.000 description 7
208000025865 Ulcer Diseases 0.000 description 7
206010012601 diabetes mellitus Diseases 0.000 description 7
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238000002266 amputation Methods 0.000 description 6
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238000007254 oxidation reaction Methods 0.000 description 6
239000000843 powder Substances 0.000 description 6
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239000011780 sodium chloride Substances 0.000 description 5
230000001464 adherent effect Effects 0.000 description 4
230000015572 biosynthetic process Effects 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
102000004169 proteins and genes Human genes 0.000 description 4
206010012665 Diabetic gangrene Diseases 0.000 description 3
229920002201 Oxidized cellulose Polymers 0.000 description 3
208000033809 Suppuration Diseases 0.000 description 3
206010000269 abscess Diseases 0.000 description 3
125000003172 aldehyde group Chemical group 0.000 description 3
239000000427 antigen Substances 0.000 description 3
102000036639 antigens Human genes 0.000 description 3
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239000008280 blood Substances 0.000 description 3
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238000004108 freeze drying Methods 0.000 description 3
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239000011734 sodium Substances 0.000 description 3
241000894006 Bacteria Species 0.000 description 2
206010010741 Conjunctivitis Diseases 0.000 description 2
LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 2
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 2
230000005856 abnormality Effects 0.000 description 2
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150000001413 amino acids Chemical class 0.000 description 2
230000001580 bacterial effect Effects 0.000 description 2
239000011324 bead Substances 0.000 description 2
230000017531 blood circulation Effects 0.000 description 2
230000036770 blood supply Effects 0.000 description 2
229910052796 boron Inorganic materials 0.000 description 2
230000000052 comparative effect Effects 0.000 description 2
150000001875 compounds Chemical class 0.000 description 2
238000011109 contamination Methods 0.000 description 2
238000001804 debridement Methods 0.000 description 2
230000003247 decreasing effect Effects 0.000 description 2
230000002950 deficient Effects 0.000 description 2
239000000428 dust Substances 0.000 description 2
210000000416 exudates and transudate Anatomy 0.000 description 2
210000002683 foot Anatomy 0.000 description 2
210000000455 fourth toe Anatomy 0.000 description 2
239000012535 impurity Substances 0.000 description 2
239000006166 lysate Substances 0.000 description 2
239000011159 matrix material Substances 0.000 description 2
KHIWWQKSHDUIBK-UHFFFAOYSA-N periodic acid Chemical compound OI(=O)(=O)=O KHIWWQKSHDUIBK-UHFFFAOYSA-N 0.000 description 2
229920000642 polymer Polymers 0.000 description 2
230000008569 process Effects 0.000 description 2
230000037390 scarring Effects 0.000 description 2
229910052708 sodium Inorganic materials 0.000 description 2
JQWHASGSAFIOCM-UHFFFAOYSA-M sodium periodate Chemical compound [Na+].[O-]I(=O)(=O)=O JQWHASGSAFIOCM-UHFFFAOYSA-M 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
239000000725 suspension Substances 0.000 description 2
210000003371 toe Anatomy 0.000 description 2
231100000397 ulcer Toxicity 0.000 description 2
239000004475 Arginine Substances 0.000 description 1
206010003210 Arteriosclerosis Diseases 0.000 description 1
208000000575 Arteriosclerosis Obliterans Diseases 0.000 description 1
208000035404 Autolysis Diseases 0.000 description 1
ZOXJGFHDIHLPTG-UHFFFAOYSA-N Boron Chemical compound [B] ZOXJGFHDIHLPTG-UHFFFAOYSA-N 0.000 description 1
229920002134 Carboxymethyl cellulose Polymers 0.000 description 1
206010057248 Cell death Diseases 0.000 description 1
241000819038 Chichester Species 0.000 description 1
QDHHCQZDFGDHMP-UHFFFAOYSA-N Chloramine Chemical compound ClN QDHHCQZDFGDHMP-UHFFFAOYSA-N 0.000 description 1
229920002307 Dextran Polymers 0.000 description 1
ZNZYKNKBJPZETN-WELNAUFTSA-N Dialdehyde 11678 Chemical compound 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
206010016228 Fasciitis Diseases 0.000 description 1
102000009123 Fibrin Human genes 0.000 description 1
108010073385 Fibrin Proteins 0.000 description 1
BWGVNKXGVNDBDI-UHFFFAOYSA-N Fibrin monomer Chemical compound CNC(=O)CNC(=O)CN BWGVNKXGVNDBDI-UHFFFAOYSA-N 0.000 description 1
206010017711 Gangrene Diseases 0.000 description 1
102000001554 Hemoglobins Human genes 0.000 description 1
108010054147 Hemoglobins Proteins 0.000 description 1
MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 1
206010020751 Hypersensitivity Diseases 0.000 description 1
206010058467 Lung neoplasm malignant 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
108090000526 Papain Proteins 0.000 description 1
208000030831 Peripheral arterial occlusive disease Diseases 0.000 description 1
206010037569 Purulent discharge Diseases 0.000 description 1
206010037660 Pyrexia Diseases 0.000 description 1
229920002472 Starch Polymers 0.000 description 1
108090001109 Thermolysin Proteins 0.000 description 1
206010046996 Varicose vein Diseases 0.000 description 1
235000018936 Vitellaria paradoxa Nutrition 0.000 description 1
239000002250 absorbent Substances 0.000 description 1
230000002745 absorbent Effects 0.000 description 1
239000008351 acetate buffer Substances 0.000 description 1
230000009858 acid secretion Effects 0.000 description 1
230000009471 action Effects 0.000 description 1
239000000654 additive Substances 0.000 description 1
208000030961 allergic reaction Diseases 0.000 description 1
239000003242 anti bacterial agent Substances 0.000 description 1
230000000844 anti-bacterial effect Effects 0.000 description 1
229940088710 antibiotic agent Drugs 0.000 description 1
229940121375 antifungal agent Drugs 0.000 description 1
ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
208000011775 arteriosclerosis disease Diseases 0.000 description 1
210000001367 artery Anatomy 0.000 description 1
230000003143 atherosclerotic effect Effects 0.000 description 1
239000003899 bactericide agent Substances 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
229920003174 cellulose-based polymer Polymers 0.000 description 1
238000006243 chemical reaction Methods 0.000 description 1
239000003795 chemical substances by application Substances 0.000 description 1
230000001684 chronic effect Effects 0.000 description 1
230000004087 circulation Effects 0.000 description 1
238000004140 cleaning Methods 0.000 description 1
239000000356 contaminant Substances 0.000 description 1
230000034994 death Effects 0.000 description 1
238000000354 decomposition reaction Methods 0.000 description 1
230000007812 deficiency Effects 0.000 description 1
238000011161 development Methods 0.000 description 1
230000018109 developmental process Effects 0.000 description 1
238000009826 distribution Methods 0.000 description 1
238000010828 elution Methods 0.000 description 1
230000002255 enzymatic effect Effects 0.000 description 1
210000000981 epithelium Anatomy 0.000 description 1
230000001747 exhibiting effect Effects 0.000 description 1
238000002474 experimental method Methods 0.000 description 1
229950003499 fibrin Drugs 0.000 description 1
239000012530 fluid Substances 0.000 description 1
239000000417 fungicide 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
210000001255 hallux Anatomy 0.000 description 1
230000035876 healing Effects 0.000 description 1
229920001477 hydrophilic polymer Polymers 0.000 description 1
230000002209 hydrophobic effect Effects 0.000 description 1
208000015181 infectious disease Diseases 0.000 description 1
230000002458 infectious effect Effects 0.000 description 1
230000002757 inflammatory effect Effects 0.000 description 1
230000005764 inhibitory process Effects 0.000 description 1
230000003993 interaction Effects 0.000 description 1
238000005342 ion exchange Methods 0.000 description 1
208000028867 ischemia Diseases 0.000 description 1
230000000670 limiting effect Effects 0.000 description 1
239000007791 liquid phase Substances 0.000 description 1
230000007774 longterm Effects 0.000 description 1
201000005202 lung cancer Diseases 0.000 description 1
208000020816 lung neoplasm Diseases 0.000 description 1
238000002803 maceration Methods 0.000 description 1
239000000203 mixture Substances 0.000 description 1
NALMPLUMOWIVJC-UHFFFAOYSA-N n,n,4-trimethylbenzeneamine oxide Chemical compound CC1=CC=C([N+](C)(C)[O-])C=C1 NALMPLUMOWIVJC-UHFFFAOYSA-N 0.000 description 1
235000015097 nutrients Nutrition 0.000 description 1
230000000414 obstructive effect Effects 0.000 description 1
238000010428 oil painting Methods 0.000 description 1
235000019834 papain Nutrition 0.000 description 1
229940055729 papain Drugs 0.000 description 1
230000002093 peripheral effect Effects 0.000 description 1
239000011148 porous material Substances 0.000 description 1
230000002265 prevention Effects 0.000 description 1
230000002035 prolonged effect Effects 0.000 description 1
235000019833 protease Nutrition 0.000 description 1
230000017854 proteolysis Effects 0.000 description 1
229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 1
238000012958 reprocessing Methods 0.000 description 1
230000000717 retained effect Effects 0.000 description 1
231100000241 scar Toxicity 0.000 description 1
210000000453 second toe Anatomy 0.000 description 1
230000028043 self proteolysis Effects 0.000 description 1
238000005549 size reduction Methods 0.000 description 1
239000012279 sodium borohydride Substances 0.000 description 1
229910000033 sodium borohydride Inorganic materials 0.000 description 1
239000011697 sodium iodate Substances 0.000 description 1
229940032753 sodium iodate Drugs 0.000 description 1
235000015281 sodium iodate Nutrition 0.000 description 1
239000007921 spray Substances 0.000 description 1
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235000019698 starch Nutrition 0.000 description 1
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229940124530 sulfonamide Drugs 0.000 description 1
150000003456 sulfonamides Chemical class 0.000 description 1
239000000454 talc Substances 0.000 description 1
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230000000699 topical effect Effects 0.000 description 1
231100000331 toxic Toxicity 0.000 description 1
230000002588 toxic effect Effects 0.000 description 1
208000027185 varicose disease Diseases 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)

JP59202175A 1983-09-29 1984-09-28 蛋白質分解性被覆物及びその製造方法 Pending JPS6094916A (ja)

Applications Claiming Priority (2)

Application Number	Priority Date	Filing Date	Title
CS7138-83		1983-09-29
CS713883A CS249311B1 (en)	1983-09-29	1983-09-29	Proteolytic wound dressing

Publications (1)

Publication Number	Publication Date
JPS6094916A true JPS6094916A (ja)	1985-05-28

Family

ID=5419947

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
JP59202175A Pending JPS6094916A (ja)	1983-09-29	1984-09-28	蛋白質分解性被覆物及びその製造方法

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)

Families Citing this family (15)

* 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
IT1395129B1 (it)	2009-07-30	2012-09-05	Franzoni Filati S P A	Aminoglicosidi ed aminoglicosidi pregelatinizzati coniugati covalentemente al cotone
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

Also Published As

Publication number	Publication date
SE8404769L (sv)	1985-03-30
DD258121A3 (de)	1988-07-13
HUT35956A (en)	1985-08-28
CA1217134A (en)	1987-01-27
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

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